Metadata-Version: 2.1
Name: brendapy
Version: 0.5.0
Summary: Parsing BRENDA information.
Home-page: https://github.com/matthiaskoenig/brendapy
Download-URL: https://pypi.org/project/brendapy
Author: Matthias Koenig
Author-email: konigmatt@googlemail.com
Maintainer: Matthias Koenig
Maintainer-email: konigmatt@googlemail.com
License: LGPL-3.0
Project-URL: Source Code, https://github.com/matthiaskoenig/brendapy
Project-URL: Documentation, https://github.com/matthiaskoenig/brendapy
Project-URL: Bug Tracker, https://github.com/matthiaskoenig/brendapy/issues
Keywords: BRENDA,enzyme kinetics,modeling
Classifier: Development Status :: 4 - Beta
Classifier: Intended Audience :: Science/Research
Classifier: License :: OSI Approved :: GNU Lesser General Public License v3 (LGPLv3)
Classifier: Operating System :: OS Independent
Classifier: Programming Language :: Python :: 3.8
Classifier: Programming Language :: Python :: 3.9
Classifier: Programming Language :: Python :: 3.10
Classifier: Topic :: Scientific/Engineering
Classifier: Topic :: Scientific/Engineering :: Bio-Informatics
Description-Content-Type: text/x-rst
Provides-Extra: development
License-File: LICENSE

.. image:: https://github.com/matthiaskoenig/brendapy/raw/develop/docs/images/favicon/brendapy-100x100-300dpi.png
   :align: left
   :alt: brendapy logo

brendapy: BRENDA in python
==========================

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   :alt: Current PyPI Version

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   :alt: Supported Python Versions

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   :alt: GNU Lesser General Public License 3

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   :alt: Zenodo DOI

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   :alt: Black

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   :alt: mypy

The :code:`brendapy` package provides a python parser and utility functions 
for enzyme information from `BRENDA <https://www.brenda-enzymes.org/index.php>`__. 
The parser extracts the all information split up by individual protein entries from the database flat file and makes it accessible in a simple manner.
:code:`brendapy` support has been tested on python :code:`py38`, :code:`py39` and :code:`py310`. Code is available from 
`https://github.com/matthiaskoenig/brendapy <https://github.com/matthiaskoenig/brendapy>`__.
 
This package was developed in the context of building kinetic pathway models with focus on extracting parameters like `Km` or `Ki` from BRENDA.


How to cite
===========
Use the following to cite `brendapy` in your project.

.. image:: https://zenodo.org/badge/DOI/10.5281/zenodo.3355000.svg
   :target: https://doi.org/10.5281/zenodo.3355000
   :alt: Zenodo DOI

If you use this package cite `BRENDA <https://www.brenda-enzymes.org/index.php>`__

::

    Chang A., Jeske L., Ulbrich S., Hofmann J., Koblitz J., Schomburg I., Neumann-Schaal M., Jahn D., Schomburg D.
    BRENDA, the ELIXIR core data resource in 2021: new developments and updates. (2021), Nucleic Acids Res., 49:D498-D508.
    DOI: 10.1093/nar/gkaa1025 PubMed: 33211880

Contributing
============

Contributions are always welcome! Please read the `contributing guidelines
<https://github.com/matthiaskoenig/brendapy/blob/develop/.github/CONTRIBUTING.rst>`__ to
get started.

License
=======

* Source Code: `LGPLv3 <http://opensource.org/licenses/LGPL-3.0>`__
* Documentation: `CC BY-SA 4.0 <http://creativecommons.org/licenses/by-sa/4.0/>`__

The brendapy source is released under both the GPL and LGPL licenses version 2 or
later. You may choose which license you choose to use the software under.

This program is free software: you can redistribute it and/or modify it under
the terms of the GNU General Public License or the GNU Lesser General Public
License as published by the Free Software Foundation, either version 2 of the
License, or (at your option) any later version.

This program is distributed in the hope that it will be useful, but WITHOUT ANY
WARRANTY; without even the implied warranty of MERCHANTABILITY or FITNESS FOR A
PARTICULAR PURPOSE. See the GNU General Public License for more details.

Funding
=======
Matthias König was supported by the Federal Ministry of Education and Research (BMBF, Germany)
within the research network Systems Medicine of the Liver (**LiSyM**, grant number 031L0054) 
and is supported by the German Research Foundation (DFG) within the Research Unit Programme FOR 5151 
"`QuaLiPerF <https://qualiperf.de>`__ (Quantifying Liver Perfusion-Function Relationship in Complex Resection - 
A Systems Medicine Approach)" by grant number 436883643 and by grant number 465194077 (Priority Programme SPP 2311, Subproject SimLivA).

Installation
============
`brendapy` is available from `pypi <https://pypi.python.org/pypi/brendapy>`__ and 
can be installed via:: 

    pip install brendapy

Develop version
---------------
The latest develop version can be installed via::

    pip install git+https://github.com/matthiaskoenig/brendapy.git@develop

Or via cloning the repository and installing via::

    git clone https://github.com/matthiaskoenig/brendapy.git
    cd brendapy
    pip install -e .

To install for development use::

    pip install -e .[development]
    
    
Usage
=====
Examples are provided in `./src/brendapy/examples.py <./src/brendapy/examples.py>`__ and `./tests/test_brendapy.py <./tests/test_brenda.py>`__.

.. code:: python

    """Example use case brendapy."""
    
    from brendapy import BrendaParser
    from brendapy.console import console
    
    
    def human_proteins_for_ec(ec: str = "1.1.1.1") -> None:
        """Parse the human protein entries for a given EC number in BRENDA.
    
        Prints overview of number of proteins, protein ids, and human proteins.
        """
        brenda = BrendaParser()
        proteins = brenda.get_proteins(ec)
    
        console.print(f"{len(proteins)} proteins for EC {ec} in BRENDA")
        console.print(f"Protein identifier: {proteins.keys()}")
        console.print("-" * 80)
        for p in proteins.values():
            if p.organism == "Homo sapiens":
                console.print(p)
                console.rule()
    
    
    if __name__ == "__main__":
        human_proteins_for_ec(ec="1.1.1.1")


.. code:: bash

    OrderedDict([('protein_id', 107),
                 ('ec', '1.1.1.1'),
                 ('organism', 'Homo sapiens'),
                 ('taxonomy', 9606),
                 ('uniprot', 'P00326'),
                 ('CF',
                  [{'comment': '#13,24,44,61,111,113,166# dependent on '
                               '<113,114,126,128,197,210,292>; #122# specific for '
                               'NAD+ <211>; #162# specific for <287>; #46,96# '
                               'dependent <153,154,159>; #163# preferred cofactor '
                               '<288>; #41# kinetics of coenzyme binding in the '
                               'pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced '
                               'conversion <62>; #41# NAD+ acts as an activator '
                               'which induces an active form of the enzyme <34>; '
                               '#41# preferred substrate <42>; #85# activity with '
                               'mutants G223D/T224I and G223D/T224I/H225N <125>; '
                               '#10# cofactor binding mode <120>; #120# dependent '
                               'on, cofactor binding mechanism and conformation '
                               'from crystal structure analysis <112>; #88# the '
                               'monomer consists of a catalytic and a '
                               'cofactor-binding domain, the cofactor is bound '
                               'between 2 domains in a cleft <127>; '
                               '#7,27,34,50,66# strongly preferred as cofactor '
                               '<135>; #93# specific for NAD+, no activity with '
                               'NADP+, pro-R stereospecificity for hydrogen '
                               'transfer <144>; #99# ADH1 preferrs NAD+ 205fold '
                               'better than NADP+ as cofactor <172>; #15# ADH3 '
                               'does not react with NADP+ <172>; #144# preferred '
                               'over NADP+ <138>; #6# strict requirement for '
                               'NAD(H) as the coenzyme. Critical role of the D37 '
                               'residue in discriminating NAD(H) from NADP(H) '
                               '<169>; #112# shows NAD+ as the preferred co-factor '
                               'over NADP+ <213>; #41# the binding of NAD+ is '
                               'kinetically limited by a unimolecular '
                               'isomerization (corresponding to the conformational '
                               'change) that is controlled by deprotonation of the '
                               'catalytic zinc-water to produce a '
                               'negatively-charged zinc-hydroxide, which can '
                               'attract the positively-charged nicotinamide ring '
                               '<198>; #115# NAD+ is prefered over NADP+ <215>; '
                               '#116# NADP+ is prefered over NAD+ <215>; #125# '
                               'strict requirement for NAD(H) as the coenzyme, no '
                               'activity with NADP+. The specificity constant '
                               'value is 6fold higher for NADH than NAD+ <218>; '
                               '#124# the enzyme transfers the deuteride to the '
                               'Si-face of NAD+ <219>; #48# Adh3 is strictly '
                               'dependent on NAD+/NADH, and shows no activity with '
                               'NADP+/NADPH as cofactor <223>; #134# exclusively '
                               'NAD+ dependent <237>; #51# 57fold preferred over '
                               'NADP+ <279>; #23# H255R single mutant exhibits an '
                               'increased binding affinity toward NADP+ and a '
                               'concomitant reduction in affinity for NAD+ <290>; '
                               '#23# insertion of an RTX domain from the adenylate '
                               'cyclase of Bordetella pertussis into a loop near '
                               'the catalytic active site of the thermostable '
                               'alcohol dehydrogenase D from Pyrococcus furiosus. '
                               'The resultant chimera, beta-AdhD, gains the '
                               'calcium-binding ability of the beta-roll, retains '
                               'the thermostable activity of AdhD, and exhibits '
                               'reduced overall alcohol dehydrogenase activity. '
                               'The addition of calcium to beta-AdhD '
                               'preferentially inhibits NAD+-dependent activity in '
                               'comparison to NADP+-dependent activity. Calcium is '
                               'a competitive inhibitor of AdhD, and the addition '
                               'of the RTX domain introduces calcium-dependent '
                               'noncompetitive inhibition to beta-AdhD affecting '
                               'NAD+-dependent activity <289>',
                    'data': 'NAD+',
                    'refs': [1,
                             2,
                             3,
                             4,
                             5,
                             6,
                             7,
                             8,
                             9,
                             10,
                             11,
                             12,
                             13,
                             14,
                             15,
                             16,
                             17,
                             18,
                             19,
                             20,
                             21,
                             22,
                             23,
                             24,
                             25,
                             26,
                             27,
                             28,
                             29,
                             30,
                             31,
                             32,
                             33,
                             34,
                             35,
                             36,
                             37,
                             38,
                             39,
                             40,
                             41,
                             42,
                             43,
                             44,
                             45,
                             46,
                             47,
                             48,
                             49,
                             50,
                             51,
                             52,
                             53,
                             54,
                             55,
                             56,
                             57,
                             58,
                             59,
                             60,
                             61,
                             62,
                             63,
                             64,
                             65,
                             66,
                             67,
                             68,
                             69,
                             70,
                             71,
                             72,
                             73,
                             74,
                             75,
                             76,
                             77,
                             78,
                             79,
                             80,
                             81,
                             82,
                             83,
                             84,
                             85,
                             86,
                             87,
                             88,
                             89,
                             90,
                             91,
                             92,
                             93,
                             94,
                             95,
                             96,
                             97,
                             98,
                             99,
                             100,
                             101,
                             102,
                             103,
                             105,
                             110,
                             111,
                             112,
                             113,
                             114,
                             115,
                             116,
                             118,
                             120,
                             121,
                             124,
                             125,
                             126,
                             127,
                             128,
                             129,
                             130,
                             135,
                             136,
                             137,
                             138,
                             139,
                             141,
                             143,
                             144,
                             146,
                             148,
                             149,
                             152,
                             153,
                             154,
                             156,
                             157,
                             158,
                             159,
                             161,
                             162,
                             163,
                             164,
                             165,
                             169,
                             172,
                             180,
                             194,
                             195,
                             196,
                             197,
                             198,
                             200,
                             201,
                             202,
                             203,
                             204,
                             205,
                             206,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             215,
                             217,
                             218,
                             219,
                             220,
                             221,
                             222,
                             223,
                             225,
                             226,
                             227,
                             229,
                             230,
                             231,
                             232,
                             233,
                             234,
                             237,
                             243,
                             252,
                             254,
                             256,
                             257,
                             260,
                             269,
                             272,
                             279,
                             286,
                             287,
                             288,
                             289,
                             290,
                             292,
                             293]}]),
                 ('ID', '1.1.1.1'),
                 ('IN',
                  [{'comment': '#100# 50% (v/v), 29% loss of activity <173>; #107# '
                               'DMSO inhibits isozyme ADH2-catalysed oxidation in '
                               'an uncompetitive mode and reduction in a mixed '
                               'mode <214>; #107# DMSO inhibits isozymes '
                               'ADH1C-catalysed oxidation in an uncompetitive mode '
                               'and reduction in a mixed mode, no inhibition is '
                               'detected with isozyme ADH3 <214>; #110# DMSO '
                               'inhibits isozymes ADH4-catalysed oxidation in an '
                               'uncompetitive mode and reduction in a mixed mode '
                               '<214>',
                    'data': 'DMSO',
                    'refs': [173, 214]},
                   {'comment': '#46# competitive inhibitor <163>; #8# 1 mM, 31% '
                               'inhibition <23>; #8# class III enzyme is '
                               'completely insensitive to inhibition <11,16>; #8# '
                               'poor inhibitor, class II isoenzyme <14>; #8# no '
                               'inhibition by 12 mM <21>; #8# competitive against '
                               'ethanol <96>; #36# isoenzyme AA-ADH, BB-ADH and '
                               'TT-ADH <95>; #5# inhibits cell protein '
                               'carbonylation following exposure to crotyl alcohol '
                               '<117>',
                    'data': '4-Methylpyrazole',
                    'refs': [2,
                             11,
                             14,
                             16,
                             21,
                             23,
                             24,
                             25,
                             95,
                             96,
                             117,
                             135,
                             163,
                             214]},
                   {'comment': '#91# substrate inhibition above 0.5 M <105>; #100# '
                               '50% (v/v), 59% loss of activity <173>; #107# '
                               'ethanol competitively inhibits the oxidation of '
                               '1-hydroxymethylpyrene by ADH1C and ADH3 <214>; '
                               '#110# ethanol competitively inhibits the oxidation '
                               'of 1-hydroxymethylpyrene by ADH4 <214>',
                    'data': 'ethanol',
                    'refs': [105, 173, 214]}]),
                 ('KI',
                  [{'chebi': 'CHEBI:16236',
                    'comment': '#107# isozyme ADH1C, using 1-hydroxymethylpyrene '
                               'as substrate <214>',
                    'data': '1.7 {ethanol}',
                    'refs': [214],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1.7},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#107# isozyme ADH3, using 1-hydroxymethylpyrene as '
                               'substrate <214>',
                    'data': '1470 {ethanol}',
                    'refs': [214],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1470.0}]),
                 ('KM',
                  [{'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.00024 {1-formyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.00024},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.00031 {1-hydroxymethyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.00031},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.00032 {1-formyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.00032},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.00037 {4-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '4-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.00037},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.00048 {2-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '2-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.00048},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.0005 {1-formylpyrene}',
                    'refs': [214],
                    'substrate': '1-formylpyrene',
                    'units': 'mM',
                    'value': 0.0005},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.00055 {1-formylpyrene}',
                    'refs': [214],
                    'substrate': '1-formylpyrene',
                    'units': 'mM',
                    'value': 0.00055},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.00057 {1-hydroxymethyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.00057},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.00059 {1-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.00059},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.00075 {1-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.00075},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.0009 {1-formyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.0009},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.001 {4-formylpyrene}',
                    'refs': [214],
                    'substrate': '4-formylpyrene',
                    'units': 'mM',
                    'value': 0.001},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.001 {4-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '4-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.001},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.00115 {1-hydroxymethyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.00115},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.00131 {1-formyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.00131},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.00149 {1-formyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.00149},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.0021 {2-formylpyrene}',
                    'refs': [214],
                    'substrate': '2-formylpyrene',
                    'units': 'mM',
                    'value': 0.0021},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.0021 {4-formylpyrene}',
                    'refs': [214],
                    'substrate': '4-formylpyrene',
                    'units': 'mM',
                    'value': 0.0021},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.0029 {2-formylpyrene}',
                    'refs': [214],
                    'substrate': '2-formylpyrene',
                    'units': 'mM',
                    'value': 0.0029},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.0038 {1-formyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.0038},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.0038 {4-formylpyrene}',
                    'refs': [214],
                    'substrate': '4-formylpyrene',
                    'units': 'mM',
                    'value': 0.0038},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.0044 {2-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '2-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.0044},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.0064 {1-hydroxymethyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.0064},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.0064 {1-hydroxymethyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.0064},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.009 {2-formylpyrene}',
                    'refs': [214],
                    'substrate': '2-formylpyrene',
                    'units': 'mM',
                    'value': 0.009},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.012 {1-formylpyrene}',
                    'refs': [214],
                    'substrate': '1-formylpyrene',
                    'units': 'mM',
                    'value': 0.012},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.04 {4-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '4-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.04},
                   {'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.059 {1-hydroxymethyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.059},
                   {'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '0.076 {1-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.076},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.106 {2-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '2-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.106},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.34 {acetaldehyde}',
                    'refs': [214],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 0.34},
                   {'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '0.39 {1-Octanol}',
                    'refs': [214],
                    'substrate': '1-Octanol',
                    'units': 'mM',
                    'value': 0.39},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#107# isozyme ADH1C, at 21-23°C <214>',
                    'data': '0.77 {ethanol}',
                    'refs': [214],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.77},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '26 {acetaldehyde}',
                    'refs': [214],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 26.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#107# isozyme ADH2, at 21-23°C <214>',
                    'data': '33 {ethanol}',
                    'refs': [214],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 33.0},
                   {'chebi': 'CHEBI:17935',
                    'comment': '#107# isozyme ADH3, at 21-23°C <214>',
                    'data': '9.6 {octanal}',
                    'refs': [214],
                    'substrate': 'octanal',
                    'units': 'mM',
                    'value': 9.6}]),
                 ('LO',
                  [{'comment': '#61# 2 isozymes <113>; #24# enzyme polymer forms '
                               'rod-like helical particles <128>',
                    'data': 'cytosol',
                    'refs': [113, 128, 135, 194, 214]}]),
                 ('MW',
                  [{'comment': '#113# SDS-PAGE <197>; #107# isozyme ADH2, apparent '
                               'molecular weight deduced from electrophoretic '
                               'mobility <214>; #110# isozyme ADH4, calculated '
                               'from amino acid sequence <214>; #93,133# 4 * '
                               '40000, SDS-PAGE <144,239>; #8,10,36,53,80# 2 * '
                               '40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,81,132# '
                               'x * 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, '
                               'ADH-3, SDS-PAGE <49>; #42# 2 * 40000, enzyme form '
                               'ADHI <68>',
                    'data': '40000',
                    'refs': [11,
                             16,
                             23,
                             24,
                             44,
                             49,
                             52,
                             59,
                             68,
                             87,
                             95,
                             144,
                             197,
                             214,
                             227,
                             239,
                             272]},
                   {'comment': '#107# isozyme ADH3, apparent molecular weight '
                               'deduced from electrophoretic mobility <214>',
                    'data': '39500',
                    'refs': [214]},
                   {'comment': '#107# isozyme ADH3, calculated from amino acid '
                               'sequence <214>',
                    'data': '39720',
                    'refs': [214]},
                   {'comment': '#107# isozyme ADH1C, calculated from amino acid '
                               'sequence <214>',
                    'data': '39870',
                    'refs': [214]},
                   {'comment': '#107# isozyme ADH2, calculated from amino acid '
                               'sequence <214>',
                    'data': '40220',
                    'refs': [214]},
                   {'comment': '#107# isozyme ADH1C, apparent molecular weight '
                               'deduced from electrophoretic mobility <214>; #110# '
                               'isozyme ADH4, apparent molecular weight deduced '
                               'from electrophoretic mobility <214>',
                    'data': '40500',
                    'refs': [214]}]),
                 ('OSS',
                  [{'comment': '#107,110# DMSO is not an ideal '
                               'substrate-delivering solvent for ADH-catalysed '
                               'reactions <214>; #151# 20% v/v, 24 h, 87% residual '
                               'activity <244>; #56# 20% v/v, 70% residual '
                               'activity <255>',
                    'data': 'DMSO',
                    'refs': [214, 244, 255]}]),
                 ('RE',
                  {'a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,41# '
                   'ordered bi-bi mechanism <31,43>; #4,76# rapid equilibrium '
                   'random mechanism <63>; #8# ordered bi bi mechanism with '
                   'cofactor adding first to form a binary enzyme complex <23>; '
                   '#41# isoenzyme EE and SS: ordered bi bi mechanism <35>; '
                   '#10,33# mechanism is predominantly ordered with ethanol, but '
                   'partially random with butanol <91>; #41# kinetic mechanism is '
                   'random for ethanol oxidation and compulsory ordered for '
                   'acetaldehyde reduction <41>; #38# oxidizes ethanol in an '
                   'ordered bi-bi mechanism with NAD+ as the first substrate fixed '
                   '<85>; #10# compulsory-order mechanism with the rate-limiting '
                   'step being the dissociation of the product enzyme-NAD+ complex '
                   '<90>; #28,68,79# Theorell-Chance mechanism <38,69,74>; #44# '
                   'sequential reaction mechanism <114>; #88# active site '
                   'structure <127>; #79# catalytic mechanism involves a proton '
                   'relay modulated by the coupled ionization of the active site '
                   'Lys155/Tyr151 pair, and a NAD+ ribose 2-OH switch, other '
                   'active site residues are Ser138 and Trp144, ionization '
                   'properties, substrate binding, overview <130>; #8# class IV '
                   'alcohol dehydrogenase also functions as retinol dehydrogenase, '
                   'reaction and kinetic mechanism: asymmetric rapid equilibrium '
                   'random mechanism with 2 dead-end ternary complexes fro retinol '
                   'oxidation and a rapid equilibrium ordered mechanism with one '
                   'dead-end ternary complex for retinal reduction, a unique '
                   'mechanistic form fro zinc-containing ADH in the medium chain '
                   'dehydrogenase/reductase superfamily of enzymes <124>; #10# '
                   'detailed determination of the reaction and kinetic mechanisms, '
                   'active site structure and determination of amino acid residues '
                   'involved in catalysis, 3 isozymes <120>; #117# ordered bibi '
                   'mechanism, structural and functional implications of amino '
                   'acid residue 47 <110>; #41# ordered sequential bibi reaction '
                   'mechanism, modeling of oxidation kinetic mechanism <117>; '
                   '#119# reaction mechanism, His51 is involved, but not '
                   'essential, in catalysis facilitating the deprotonation of the '
                   'hydroxyl group of water or alcohol ligated to the catalytic '
                   'zinc <111>; #8# Ser48 is involved in catalysis, isozyme '
                   'gamma(2)gamma(2) <109>; #27# the catalytic triad consists of '
                   'Cys44, His67, and Cys154, active site structure <129>)',
                   'a secondary alcohol + NAD+ = a ketone + NADH + H+'}),
                 ('RN', {'alcohol dehydrogenase'}),
                 ('RT', {'redox reaction', 'reduction', 'oxidation'}),
                 ('SN', {'alcohol:NAD+ oxidoreductase'}),
                 ('SP',
                  [{'data': '1-hydroxymethyl-6-methylpyrene + NAD+ = '
                            '1-formyl-6-methylpyrene + NADH + H+ {r}',
                    'refs': [214]},
                   {'data': '1-hydroxymethyl-8-methylpyrene + NAD+ = '
                            '1-formyl-8-methylpyrene + NADH + H+ {r}',
                    'refs': [214]},
                   {'data': '1-hydroxymethylpyrene + NAD+ = 1-formylpyrene + NADH '
                            '+ H+ {r}',
                    'refs': [214]},
                   {'data': '2-hydroxymethylpyrene + NAD+ = 2-formylpyrene + NADH '
                            '+ H+ {r}',
                    'refs': [214]},
                   {'data': '4-hydroxymethylpyrene + NAD+ = 4-formylpyrene + NADH '
                            '+ H+ {r}',
                    'refs': [214]},
                   {'comment': '#48# best substrate <223>; #79,112# 100% activity '
                               '<61,213>; #101# no activity with NADP+, in reverse '
                               'reaction no activity with NADPH <171>; #31# the '
                               'enzyme is highly specific for ethanol with NAD+ as '
                               'the coenzyme <181>; #113# 88% activity compared to '
                               'cyclohexanol <197>; #107# substrate for isozyme '
                               'ADH1C, extremely poor substrate for isozyme ADH3 '
                               '<214>; #107# substrate for isozyme ADH2 <214>; '
                               '#110# substrate for isozyme ADH4 <214>; #134# the '
                               'enzyme shows a preference for short-chain alcohols '
                               'ethanol and 1-propanol <237>; #155# 12% of the '
                               'activity with butan-1-ol <271>; #161# 33% of the '
                               'activity with 1,4-butanediol <286>) |#120# 83% of '
                               'the activity with butan-2-ol <256>',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH + H+',
                    'refs': [61,
                             66,
                             79,
                             85,
                             103,
                             136,
                             139,
                             140,
                             143,
                             144,
                             147,
                             148,
                             153,
                             159,
                             161,
                             162,
                             163,
                             171,
                             173,
                             174,
                             181,
                             194,
                             195,
                             196,
                             197,
                             203,
                             205,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             222,
                             223,
                             231,
                             233,
                             237,
                             239,
                             246,
                             252,
                             256,
                             271,
                             277,
                             279,
                             284,
                             286,
                             288]},
                   {'comment': '#48# best substrate <223>; #79,112# 100% activity '
                               '<61,213>; #101# no activity with NADP+, in reverse '
                               'reaction no activity with NADPH <171>; #31# the '
                               'enzyme is highly specific for ethanol with NAD+ as '
                               'the coenzyme <181>; #113# 88% activity compared to '
                               'cyclohexanol <197>; #107# substrate for isozyme '
                               'ADH1C, extremely poor substrate for isozyme ADH3 '
                               '<214>; #107# substrate for isozyme ADH2 <214>; '
                               '#110# substrate for isozyme ADH4 <214>; #134# the '
                               'enzyme shows a preference for short-chain alcohols '
                               'ethanol and 1-propanol <237>; #155# 12% of the '
                               'activity with butan-1-ol <271>; #161# 33% of the '
                               'activity with 1,4-butanediol <286>) |#120# 83% of '
                               'the activity with butan-2-ol <256>| {r',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH + H+',
                    'refs': [61,
                             66,
                             79,
                             85,
                             103,
                             136,
                             139,
                             140,
                             143,
                             144,
                             147,
                             148,
                             153,
                             159,
                             161,
                             162,
                             163,
                             171,
                             173,
                             174,
                             181,
                             194,
                             195,
                             196,
                             197,
                             203,
                             205,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             222,
                             223,
                             231,
                             233,
                             237,
                             239,
                             246,
                             252,
                             256,
                             271,
                             277,
                             279,
                             284,
                             286,
                             288]},
                   {'comment': '#13# broad substrate specificity <126>; #10# '
                               'constitutive enzyme <94>; #42# key enzyme in '
                               'ethanol production <68>; #52# one constitutive '
                               'enzyme, ADH-MI and one inducible enzyme, ADH-MII '
                               '<82>; #53# enzyme may be involved in the '
                               'metabolism of dietary wax esters in salmonid fish '
                               '<59>; #79# the enzyme oxidizes alcohols to '
                               'aldehydes or ketones both for detoxification and '
                               'metabolic purposes <38>; #36# involvement in the '
                               'development of male hamster reproductive system '
                               '<47>; #89# enzyme shows high substrate specificity '
                               'towards primary aliphatic alcohols, no activity '
                               'with 2-butanol, tert-butanol, isoamyl alcohol, '
                               'isobutyl alcohol, 1,6-hexadiol, and mono-, di-, '
                               'and triethanolamine <118>; #91# no activity with '
                               'methanol, 2-propanol, and isoamyl alcohol <105>; '
                               '#10# substrate specificity and stereospecificity, '
                               'substrate binding pocket structure of the 3 '
                               'isozymes, involving Met294, Trp57, and Trp93 '
                               '<120>; #61# substrate specificity of the 2 '
                               'isozmyes with various substrates, overview, '
                               'isozymes are highly specific for the '
                               '(R)-stereoisomers and enantioselctive for the '
                               'R(-)isomers <113>; #106# the enzyme undergoes a '
                               'substantial conformational change in the apo-holo '
                               'transition, accompanied by loop movements at the '
                               'domain interface <108>; #60# alcohol dehydrogenase '
                               'activity may not limit alcohol supply for ester '
                               'production during ripening <146>; #54# Cm-ADH2 '
                               'cannot reduce branched aldehydes <151>; #10# '
                               'effects of pressure on deuterium isotope effects '
                               'of yeast alcohol dehydrogenase using alternative '
                               'substrates <139>; #93# no activity with methanol '
                               '<144>; #94# the enzyme does not act on short-chain '
                               'normal alkyl alcohols, including methanol and '
                               'ethanol <137>; #97# no activity towards methanol, '
                               'ethanol, 1-propanol, triethylene glycol, '
                               'polyethylene glycol 400, polyethylene glycol 1000, '
                               'D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, '
                               'propionaldehyde, butyraldehyde, and valeraldehyde '
                               '<156>; #99# ADH1 preferrs primary alcohols '
                               'containing C3-C8 carbons to secondary alcohols '
                               'such as 2-propanol and 2-butanol. ADH1 possesses '
                               'specific carboxylate ester-forming activity <172>; '
                               '#102# no activity detected with: '
                               'N-benzyl-2-pyrrolidinone, 2-pyrrolidinone, '
                               '3-hexanone, 4-hydroxy-2-butanone, '
                               '(R)-N-benzyl-3-pyrrolidinol, ethanol, '
                               '1,3-propanediol, 1-butanol, 1,4-butanediol, '
                               '1,2,3-butanetriol, 1,2,4-butanetriol, acetol, '
                               '2-phenyl-1-propanol, 3-phenyl-1-propanol, benzyl '
                               'alcohol and glycerol. No activity with NADP+ or '
                               'NADPH <185>; #6# preference for reduction of '
                               'aromatic ketones and alpha-keto esters, and poor '
                               'activity on aromatic alcohols and aldehydes <169>; '
                               '#26# when NADH is replaced with NADPH, the '
                               'reaction rate is reduced by 0.6% <188>; #41# '
                               'activity is severely reduced towards aliphatic '
                               'alcohols of more than 8 carbon atoms for the free '
                               'enzyme, but not so with immobilized HLAD, '
                               'exhibiting an activity towards C22 and C24 '
                               'aliphatic alcohols higher than 50% of the highest '
                               'value, obtained with C8 <204>; #8# differences in '
                               'the activities of total ADH and class I ADH '
                               'isoenzyme between cancer liver tissues and healthy '
                               'hepatocytes may be a factor in ethanol metabolism '
                               'disorders, which can intensify carcinogenesis '
                               '<180>; #113# TADH is a NAD(H)-dependent enzyme and '
                               'shows a very broad substrate spectrum producing '
                               'exclusively the (S)-enantiomer in high '
                               'enantiomeric excess (more than 99%) during '
                               'asymmetric reduction of ketones <197>; #107# '
                               '1-octanal is no substrate for isozyme ADH1C <214>; '
                               '#107# 1-octanal is no substrate for isozyme ADH2 '
                               '<214>; #110# 1-octanal is no substrate for isozyme '
                               'ADH4 <214>; #113# ADH exhibits a clear preference '
                               'for primary alcohols and corresponding aldehydes '
                               'for aliphatic substrates, in the oxidative '
                               'direction activity steeply increases with chain '
                               'length until 1-propanol and then decreases '
                               'slightly again with growing chain length, '
                               'alpha,beta-unsaturated ketones like 3-penten-2-one '
                               'and cyclohexenone are not converted by ADH, almost '
                               'no conversion of methanol (0.2%) and (+)-carvone '
                               '(0.4%) is detected <197>; #122# no activity is '
                               'detected using 1 mM NADP+ <211>; #111# no activity '
                               'towards methanol <210>; #115# substrates are a '
                               'broad range of alkyl alcohols from ethanol to '
                               '1-triacontanol <215>; #124# the physiological '
                               'direction of the catalytic reaction is reduction '
                               'rather than oxidation <219>; #125# the enzyme '
                               'displays a preference for the reduction of '
                               'alicyclic, bicyclic and aromatic ketones and '
                               'alpha-ketoesters, but is poorly active on '
                               'aliphatic, cyclic and aromatic alcohols, showing '
                               'no activity on aldehydes <218>; #124# the enzyme '
                               'shows no activity on aliphatic linear and branched '
                               'alcohols, except for a poor activity on '
                               '2-propyn-1-ol, 3-methyl-1-butanol and 2-pentanol; '
                               'however, it shows a discrete activity on aliphatic '
                               'cyclic and bicyclic alcohols. Benzyl alcohol and '
                               '4-bromobenzyl alcohol are not found to be '
                               'substrates. The S and R enantiomers of '
                               'a-(trifluoromethyl)benzyl alcohol and methyl and '
                               'ethyl mandelates show no apparent activity with '
                               'SaADH. The enzyme shows poor activity on '
                               '(+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol '
                               'and the two enantiomers of 1-(2-naphthyl)ethanol. '
                               'The enzyme is not active on aliphatic and aromatic '
                               'aldehydes, and on aliphatic linear, branched and '
                               'cyclic ketones except for 3-methylcyclohexanone. '
                               'Catalytic inactivity is observed with acetophenone '
                               'and (S)-a-(trifluoromethyl)benzyl <219>; #128# '
                               'methanol, formaldehyde, and acetone are no '
                               'substrates for HpADH3 <222>; #48# no activity with '
                               'methanol, 1-butanol, glycerol or 2-propanol <223>; '
                               '#129# substrate specificity and '
                               'enantiospecificity, overview. The (R)-specific '
                               'alcohol dehydrogenase requires NADH and reduces '
                               'various kinds of carbonyl compounds, including '
                               'ketones and aldehydes. AFPDH reduces '
                               'acetylpyridine derivatives, beta-keto esters, and '
                               'some ketones compounds with high '
                               'enantiospecificity, overview. No activity with '
                               '2-chlorobenzaldehyde and 2-tetralone, poor '
                               'activity with 1-tetralone, pyruvate, '
                               '2-oxobutyrate, oxalacetate, cyclopentanone, '
                               'cyclohexanone, cycloheptanone, and dipropylketone. '
                               'No activity with 1,2-propanediol, '
                               '3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol, '
                               'glycerol, 1-pentanol, poor activity with '
                               '1-butanol, 1-propanol, ethanol, and methanol '
                               '<225>; #86# the enzyme exhibits broad substrate '
                               'specificity towards aliphatic ketones, '
                               'cycloalkanones, aromatic ketones, and ketoesters '
                               '<226>; #133# the enzyme shows broad substrate '
                               'specificity and prefers aliphatic alcohols and '
                               'ketones. There are no large differences in the '
                               'reactivities between primary and secondary '
                               'alcohols. The enzyme produces (S)-alcohols from '
                               'the corresponding ketones. The values of the '
                               'enantiomeric excess increase with the increase of '
                               'chain length except for the reduction of '
                               '2-hexanone. The highest enantioselectivity is '
                               'shown with the reduction of 2-nonanone <239>; '
                               '#134# the NAD+-dependent HvADH1 shows a preference '
                               'for short-chain alcohols, no activity with '
                               'methanol <237>; #144# broad substrate specificity '
                               'with a preference for the reduction of ketones and '
                               'the oxidation of secondary alcohols <138>; #125# '
                               'enzyme displays a preference for the reduction of '
                               'alicyclic, bicyclic and aromatic ketones and '
                               'alpha-keto esters, but is poorly active on '
                               'aliphatic, cyclic and aromatic alcohols, and shows '
                               'no activity on aldehydes <219>; #150# enzyme '
                               'reduces aldehydes to (R)-alcohols with more than '
                               '99.8% enantiomeric excess <243>; #151# enzyme '
                               'selectively reduces the C=O bond of allylic '
                               'aldehydes/ketones to the corresponding '
                               'alpha,beta-unsaturated alcohols and also has the '
                               'capacity of stereoselectively reducing aromatic '
                               'ketones to (S)-enantioselective alcohols. The '
                               'enzyme preferentially catalyzes oxidation of '
                               'allylic/benzyl aldehydes <244>; #71# ethanol '
                               'dehydrogenase activity of Thermoanaerobium brockii '
                               'is both NAD and NADP linked, reversible, and not '
                               'inhibited by low levels of reaction products '
                               '<103>; #120,143# mutation at the substrate-binding '
                               'site, or at a dimer interface, alters kinetic '
                               'properties and protein oligomeric structure, '
                               'active site flexibility is correlated with subunit '
                               'interactions 20 A away <260>; #6# the enzyme '
                               'transfers the pro-S hydrogen of [4R-(2)H]NADH and '
                               'exhibits Prelog specificity <269>; #41# acycloNAD+ '
                               'i.e. NAD+-analogue, where the nicotinamide ribosyl '
                               'moiety has been replaced by the nicotinamide '
                               '(2-hydroxyethoxy)methyl moiety. There is no '
                               'detectable reduction of acycloNAD+ by secondary '
                               'alcohols although these alcohols serve as '
                               'competitive inhibitors. AcycloNAD+ converts horse '
                               'liver ADH from a broad spectrum alcohol '
                               'dehydrogenase, capable of utilizing either primary '
                               'or secondary alcohols, into an exclusively primary '
                               'alcohol dehydrogenase <275>; #51# bifunctional '
                               'enzyme consisting of an N-terminal acetaldehyde '
                               'dehydrogenase (ALDH) and a C-terminal alcohol '
                               'dehydrogenase (ADH). The specificity constant '
                               '(kcat/Km) is 47fold higher for acetaldehyde '
                               'reductase than that for ethanol dehydrogenase '
                               '<279>; #153# enzyme is an alcohol dehydrogenase '
                               'with additional activity for all-trans-retinol, '
                               'reaction of EC 1.1.1.184 <272>; #155# enzyme shows '
                               'activity as a reductase specific for (S)-acetoin, '
                               'EC 1.1.1.76, and both diacetyl reductase (EC '
                               '1.1.1.304) and NAD+-dependent alcohol '
                               'dehydrogenase (EC 1.1.1.1) activities <271>; #160# '
                               'the enzyme additionally catalyzes selective '
                               'reduction of 3-quinuclidinone to '
                               '(R)-3-quinuclidinol, with 84% ee and 62% '
                               'conversion after 22 h <274>; #162# Candida '
                               'albicans ADH1 is a bifunctional enzyme that '
                               'catalyzes methylglyoxal oxidation and reduction, '
                               'cf. EC 1.2.1.23 <287>; #161# the enzyme catalyzes '
                               'NAD(H)-dependent oxidation of various alcohols and '
                               'reduction of aldehydes, with a marked preference '
                               'for substrates with functional group at the '
                               'terminal carbon atom <286>; #166# almost no '
                               'activity with D-arabinonate, D-lyxonate, '
                               'D-galactonate, glycerol, meso-erythritol, '
                               'D-ribitol, D-arabitol, D-xylitol, and D-mannitol. '
                               'No activity with propanal, butanal, hexanal, and '
                               '4-oxobutanoic acid <292>; #165# the enzyme '
                               'catalyzes the reduction of acetophenone '
                               'derivatives to the corresponding (S)-chiral '
                               'alcohols in an enantiomerically pure form. The '
                               'substituents on the benzene ring of the aryl '
                               'ketones exert some effect on the enzyme activity, '
                               'although the influence is not dramatic. The '
                               'enantioselectivity of the reduction is not '
                               'affected by the substituents and pattern of the '
                               'substitution. The alpha-chlorinated acetophenone '
                               'shows a much higher activity than the '
                               'unsubstituted one (more than 10 times) <294>',
                    'data': 'more = ?',
                    'refs': [38,
                             47,
                             59,
                             68,
                             82,
                             94,
                             103,
                             105,
                             108,
                             113,
                             118,
                             120,
                             126,
                             137,
                             138,
                             139,
                             144,
                             146,
                             151,
                             156,
                             169,
                             172,
                             180,
                             185,
                             188,
                             197,
                             204,
                             210,
                             211,
                             214,
                             215,
                             218,
                             219,
                             222,
                             223,
                             225,
                             226,
                             237,
                             239,
                             243,
                             244,
                             260,
                             269,
                             271,
                             272,
                             274,
                             275,
                             279,
                             286,
                             287,
                             292,
                             294]},
                   {'comment': '#94# 33% of the activity with 2-propanol, in the '
                               'reverse reaction 435% of the activity with phenyl '
                               'trifluoromethyl ketone <137>; #97# 11% activity '
                               'compared to benzyl alcohol <156>; #99# about 85% '
                               'of activity with ethanol, ADH1 <172>; #113# 57% '
                               'activity compared to cyclohexanol <197>; #107# '
                               'substrate for isozyme ADH3 <214>',
                    'data': '1-octanol + NAD+ = octanal + NADH + H+',
                    'refs': [137, 144, 156, 172, 197, 210, 214, 222, 286]},
                   {'comment': '#94# 33% of the activity with 2-propanol, in the '
                               'reverse reaction 435% of the activity with phenyl '
                               'trifluoromethyl ketone <137>; #97# 11% activity '
                               'compared to benzyl alcohol <156>; #99# about 85% '
                               'of activity with ethanol, ADH1 <172>; #113# 57% '
                               'activity compared to cyclohexanol <197>; #107# '
                               'substrate for isozyme ADH3 <214>) {r',
                    'data': '1-octanol + NAD+ = octanal + NADH + H+',
                    'refs': [137, 144, 156, 172, 197, 210, 214, 222, 286]}]),
                 ('ST',
                  [{'bto': 'BTO:0000759',
                    'comment': '#5# isoenzyme A2 and B2 <48>; #36# isoenzyme '
                               'AA-ADH and BB-ADH most abundant in <95>; #8# '
                               'isozyme ADH1C*2 <116>; #9# females show 70% higher '
                               'hepatic alcohol dehydrogenase activity and display '
                               '60% lower voluntary ethanol intake than males. '
                               'Following ethanol administration (1 g/kg ip), '
                               'females generate a transient blood acetaldehyde '
                               'increase with levels that are 2.5fold greater than '
                               'in males. Castration of males leads to an increase '
                               'alcohol dehydrogenase activity the appearance of '
                               'an acetaldehyde burst a reduction of voluntary '
                               'ethanol intake comparable with that of females '
                               '<167>; #8# the activities of total alcohol '
                               'dehydrogenase, aldehyde dehydrogenase and class I '
                               'alcohol dehydrogenase isoenzyme between cancer '
                               'liver tissues and healthy hepatocytes might be a '
                               'factor in ethanol metabolism disorders which can '
                               'intensify carcinogenesis <186>; #107# isozymes '
                               'ADH1C and ADH3 <214>; #8# most abundant in the '
                               'liver <180>; #8# the total alcohol dehydrogenase '
                               'activity is significantly higher in cancer tissues '
                               'than in healthy liver <194>; #132# class III ADH '
                               '<227>',
                    'data': 'liver',
                    'refs': [1,
                             2,
                             5,
                             10,
                             12,
                             13,
                             14,
                             15,
                             16,
                             17,
                             18,
                             19,
                             20,
                             21,
                             22,
                             23,
                             24,
                             25,
                             26,
                             27,
                             28,
                             29,
                             30,
                             31,
                             32,
                             33,
                             34,
                             35,
                             36,
                             37,
                             39,
                             40,
                             41,
                             42,
                             44,
                             45,
                             46,
                             48,
                             49,
                             51,
                             52,
                             54,
                             55,
                             59,
                             60,
                             86,
                             92,
                             93,
                             95,
                             98,
                             101,
                             111,
                             116,
                             117,
                             143,
                             167,
                             175,
                             178,
                             180,
                             186,
                             194,
                             198,
                             200,
                             201,
                             204,
                             205,
                             212,
                             214,
                             224,
                             227,
                             275]},
                   {'bto': 'BTO:0003833',
                    'comment': '#107,110# isozyme ADH4 <214>',
                    'data': 'buccal mucosa',
                    'refs': [214]}]),
                 ('SY',
                  [{'comment': '#10,107# isozyme <202,214>',
                    'data': 'ADH2',
                    'refs': [110,
                             123,
                             128,
                             162,
                             170,
                             202,
                             214,
                             215,
                             233,
                             240,
                             252]},
                   {'comment': '#107# isozyme <214>',
                    'data': 'ADH1C',
                    'refs': [214]},
                   {'comment': '#107# isozyme <214>',
                    'data': 'ADH3',
                    'refs': [141, 172, 177, 200, 214, 252, 263]}]),
                 ('references',
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                                 'KOD1 for enantioselective bioconversion of '
                                 'aromatic secondary alcohols. Appl. Environ. '
                                 'Microbiol. (2013) 79, 2209-2217.',
                         'pubmed': 23354700},
                   244: {'info': 'Ying, X.; Wang, Y.; Xiong, B.; Wu, T.; Xie, L.; '
                                 'Yu, M.; Wang, Z.: Characterization of an '
                                 'allylic/benzyl alcohol dehydrogenase from '
                                 'Yokenella sp. strain WZY002, an organism '
                                 'potentially useful for the synthesis of '
                                 'alpha,beta-unsaturated alcohols from allylic '
                                 'aldehydes and ketones. Appl. Environ. Microbiol. '
                                 '(2014) 80, 2399-2409.',
                         'pubmed': 24509923},
                   246: {'info': 'Kirmair, L.; Seiler, D.L.; Skerra, A.: Stability '
                                 'engineering of the Geobacillus '
                                 'stearothermophilus alcohol dehydrogenase and '
                                 'application for the synthesis of a polyamide 12 '
                                 'precursor. Appl. Microbiol. Biotechnol. (2015) '
                                 '99, 10501-10513.',
                         'pubmed': 26329849},
                   252: {'info': 'Liang, J.J.; Zhang, M.L.; Ding, M.; Mai, Z.M.; '
                                 'Wu, S.X.; Du, Y.; Feng, J.X.: Alcohol '
                                 'dehydrogenases from Kluyveromyces marxianus: '
                                 'heterologous expression in Escherichia coli and '
                                 'biochemical characterization. BMC Biotechnol. '
                                 '(2014) 14, 45.',
                         'pubmed': 24885162},
                   254: {'info': 'Kontani, A.; Masuda, M.; Matsumura, H.; '
                                 'Nakamura, N.; Yohda, M.; Ohno, H.: A bioanode '
                                 'using thermostable alcohol dehydrogenase for an '
                                 'ethanol biofuel cell operating at high '
                                 'temperatures. Electroanalysis (2014) 26, '
                                 '682-686.'},
                   255: {'info': 'Willies, S.; Isupov, M.; Littlechild, J.: '
                                 'Thermophilic enzymes and their applications in '
                                 'biocatalysis: a robust aldo-keto reductase. '
                                 'Environ. Technol. (2010) 31, 1159-1167.',
                         'pubmed': 20718298},
                   256: {'info': 'Guagliardi, A.; Martino, M.; Iaccarino, I.; De '
                                 'Rosa, M.; Rossi, M.; Bartolucci, S.: '
                                 'Purification and characterization of the alcohol '
                                 'dehydrogenase from a novel strain of Bacillus '
                                 'stearothermophilus growing at 70°C. Int. J. '
                                 'Biochem. Cell Biol. (1996) 28, 239-246.',
                         'pubmed': 8729010},
                   257: {'info': 'Meadows, C.W.; Tsang, J.E.; Klinman, J.P.: '
                                 'Picosecond-resolved fluorescence studies of '
                                 'substrate and cofactor-binding domain mutants in '
                                 'a thermophilic alcohol dehydrogenase uncover an '
                                 'extended network of communication. J. Am. Chem. '
                                 'Soc. (2014) 136, 14821-14833.',
                         'pubmed': 25314615},
                   260: {'info': 'Nagel, Z.D.; Cun, S.; Klinman, J.P.: '
                                 'Identification of a long-range protein network '
                                 'that modulates active site dynamics in '
                                 'extremophilic alcohol dehydrogenases. J. Biol. '
                                 'Chem. (2013) 288, 14087-14097.',
                         'pubmed': 23525111},
                   263: {'info': 'Xiao, S.; Xu, J.; Chen, X.; Li, X.; Zhang, Y.; '
                                 'Yuan, Z.: 3-Methyl-1-butanol biosynthesis in an '
                                 'engineered Corynebacterium glutamicum. Mol. '
                                 'Biotechnol. (2016) 58, 311-318.',
                         'pubmed': 26961908},
                   269: {'info': 'Pennacchio, A.; Giordano, A.; Esposito, L.; '
                                 'Langella, E.; Rossi, M.; Raia, C.A.: Insight '
                                 'into the stereospecificity of short-chain '
                                 'thermus thermophilus alcohol dehydrogenase '
                                 'showing pro-S hydride transfer and prelog '
                                 'enantioselectivity. Protein Pept. Lett. (2010) '
                                 '17, 437-443.',
                         'pubmed': 19807673},
                   271: {'info': 'Takeda, M.; Anamizu, S.; Motomatsu, S.; Chen, '
                                 'X.; Thapa Chhetri, R.: Identification and '
                                 'characterization of a mycobacterial '
                                 'NAD+-dependent alcohol dehydrogenase with '
                                 'superior reduction of diacetyl to (S)-acetoin. '
                                 'Biosci. Biotechnol. Biochem. (2014) 78, '
                                 '1879-1886.',
                         'pubmed': 25082080},
                   272: {'info': 'Hong, S.H.; Ngo, H.P.; Kang, L.W.; Oh, D.K.: '
                                 'Characterization of alcohol dehydrogenase from '
                                 'Kangiella koreensis and its application to '
                                 'production of all-trans-retinol. Biotechnol. '
                                 'Lett. (2015) 37, 849-856.',
                         'pubmed': 25481533},
                   274: {'info': 'Spickermann, D.; Hausmann, S.; Degering, C.; '
                                 'Schwaneberg, U.; Leggewie, C.: Engineering of '
                                 'highly selective variants of Parvibaculum '
                                 'lavamentivorans alcohol dehydrogenase. '
                                 'ChemBioChem (2014) 15, 2050-2052.',
                         'pubmed': 25169816},
                   275: {'info': 'Malver, O.; Sebastian, M.J.; Oppenheimer, N.J.: '
                                 'Alteration in substrate specificity of horse '
                                 'liver alcohol dehydrogenase by an acyclic '
                                 'nicotinamide analog of NAD(+). DNA Repair (2014) '
                                 '23, 95-100.',
                         'pubmed': 25280628},
                   277: {'info': 'Moosavi-Movahedi, F.; Saboury, A.A.; Alijanvand, '
                                 'H.H.; Bohlooli, M.; Salami, M.; '
                                 'Moosavi-Movahedi, A.A.: Thermal inactivation and '
                                 'conformational lock studies on horse liver '
                                 'alcohol dehydrogenase: structural mechanism. '
                                 'Int. J. Biol. Macromol. (2013) 58, 66-72.',
                         'pubmed': 23548863},
                   279: {'info': 'Tsuji, K.; Yoon, K.S.; Ogo, S.: Biochemical '
                                 'characterization of a bifunctional '
                                 'acetaldehyde-alcohol dehydrogenase purified from '
                                 'a facultative anaerobic bacterium Citrobacter '
                                 'sp. S-77. J. Biosci. Bioeng. (2016) 121, '
                                 '253-258.',
                         'pubmed': 26216639},
                   284: {'info': 'Cheng, F.; Hu, T.; An, Y.; Huang, J.; Xu, Y.: '
                                 'Purification and enzymatic characterization of '
                                 'alcohol dehydrogenase from Arabidopsis thaliana. '
                                 'Protein Expr. Purif. (2013) 90, 74-77.',
                         'pubmed': 23707506},
                   286: {'info': 'Ashraf, R.; Rashid, N.; Kanai, T.; Imanaka, T.; '
                                 'Akhtar, M.: Pcal_1311, an alcohol dehydrogenase '
                                 'homologue from Pyrobaculum calidifontis, '
                                 'displays NADH-dependent high aldehyde reductase '
                                 'activity. Extremophiles (2017) 21, 1101-1110.',
                         'pubmed': 29022135},
                   287: {'info': 'Kwak, M.K.; Ku, M.; Kang, S.O.: NAD+-linked '
                                 'alcohol dehydrogenase 1 regulates methylglyoxal '
                                 'concentration in Candida albicans. FEBS Lett. '
                                 '(2014) 588, 1144-1153.',
                         'pubmed': 24607541},
                   288: {'info': 'Tsuji, K.; Yoon, K.S.; Ogo, S.: Biochemical '
                                 'characterization of a bifunctional '
                                 'acetaldehyde-alcohol dehydrogenase purified from '
                                 'a facultative anaerobic bacterium Citrobacter '
                                 'sp. S-77. J. Biosci. Bioeng. (2016) 121, '
                                 '253-258.',
                         'pubmed': 26216639},
                   289: {'info': 'Abdallah, W.; Solanki, K.; Banta, S.: Insertion '
                                 'of a calcium-responsive beta-roll domain into a '
                                 'thermostable alcohol dehydrogenase enables '
                                 'tunable control over cofactor selectivity. ACS '
                                 'Catal. (2018) 8, 1602-1613.'},
                   290: {'info': 'Campbell, E.; Wheeldon, I.; Banta, S.: '
                                 'Broadening the cofactor specificity of a '
                                 'thermostable alcohol dehydrogenase using '
                                 'rational protein design introduces novel kinetic '
                                 'transient behavior. Biotechnol. Bioeng. (2010) '
                                 '107, 763-774.',
                         'pubmed': 20632378},
                   292: {'info': 'Beer, B.; Pick, A.; Doering, M.; Lommes, P.; '
                                 'Sieber, V.: Substrate scope of a dehydrogenase '
                                 'from Sphingomonas species A1 and its potential '
                                 'application in the synthesis of rare sugars and '
                                 'sugar derivatives. Microb. Biotechnol. (2018) '
                                 '11, 747-758.',
                         'pubmed': 29697194},
                   293: {'info': 'Solanki, K.; Abdallah, W.; Banta, S.: '
                                 'Engineering the cofactor specificity of an '
                                 'alcohol dehydrogenase via single mutations or '
                                 "insertions distal to the 2'-phosphate group of "
                                 'NADP(H). Protein Eng. Des. Sel. (2017) 30, '
                                 '373-380.',
                         'pubmed': 28201792},
                   294: {'info': 'Zhu, D.; Malik, H.; Hua, L.: Asymmetric ketone '
                                 'reduction by a hyperthermophilic alcohol '
                                 'dehydrogenase. The substrate specificity, '
                                 'enantioselectivity and tolerance of organic '
                                 'solvents. Tetrahedron Asymmetry (2006) 17, '
                                 '3010-3014.'}}),
                 ('tissues', {'BTO:0000759', 'BTO:0003833'})])
    ──────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────
    OrderedDict([('protein_id', 110),
                 ('ec', '1.1.1.1'),
                 ('organism', 'Homo sapiens'),
                 ('taxonomy', 9606),
                 ('uniprot', 'P08319'),
                 ('CF',
                  [{'comment': '#13,24,44,61,111,113,166# dependent on '
                               '<113,114,126,128,197,210,292>; #122# specific for '
                               'NAD+ <211>; #162# specific for <287>; #46,96# '
                               'dependent <153,154,159>; #163# preferred cofactor '
                               '<288>; #41# kinetics of coenzyme binding in the '
                               'pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced '
                               'conversion <62>; #41# NAD+ acts as an activator '
                               'which induces an active form of the enzyme <34>; '
                               '#41# preferred substrate <42>; #85# activity with '
                               'mutants G223D/T224I and G223D/T224I/H225N <125>; '
                               '#10# cofactor binding mode <120>; #120# dependent '
                               'on, cofactor binding mechanism and conformation '
                               'from crystal structure analysis <112>; #88# the '
                               'monomer consists of a catalytic and a '
                               'cofactor-binding domain, the cofactor is bound '
                               'between 2 domains in a cleft <127>; '
                               '#7,27,34,50,66# strongly preferred as cofactor '
                               '<135>; #93# specific for NAD+, no activity with '
                               'NADP+, pro-R stereospecificity for hydrogen '
                               'transfer <144>; #99# ADH1 preferrs NAD+ 205fold '
                               'better than NADP+ as cofactor <172>; #15# ADH3 '
                               'does not react with NADP+ <172>; #144# preferred '
                               'over NADP+ <138>; #6# strict requirement for '
                               'NAD(H) as the coenzyme. Critical role of the D37 '
                               'residue in discriminating NAD(H) from NADP(H) '
                               '<169>; #112# shows NAD+ as the preferred co-factor '
                               'over NADP+ <213>; #41# the binding of NAD+ is '
                               'kinetically limited by a unimolecular '
                               'isomerization (corresponding to the conformational '
                               'change) that is controlled by deprotonation of the '
                               'catalytic zinc-water to produce a '
                               'negatively-charged zinc-hydroxide, which can '
                               'attract the positively-charged nicotinamide ring '
                               '<198>; #115# NAD+ is prefered over NADP+ <215>; '
                               '#116# NADP+ is prefered over NAD+ <215>; #125# '
                               'strict requirement for NAD(H) as the coenzyme, no '
                               'activity with NADP+. The specificity constant '
                               'value is 6fold higher for NADH than NAD+ <218>; '
                               '#124# the enzyme transfers the deuteride to the '
                               'Si-face of NAD+ <219>; #48# Adh3 is strictly '
                               'dependent on NAD+/NADH, and shows no activity with '
                               'NADP+/NADPH as cofactor <223>; #134# exclusively '
                               'NAD+ dependent <237>; #51# 57fold preferred over '
                               'NADP+ <279>; #23# H255R single mutant exhibits an '
                               'increased binding affinity toward NADP+ and a '
                               'concomitant reduction in affinity for NAD+ <290>; '
                               '#23# insertion of an RTX domain from the adenylate '
                               'cyclase of Bordetella pertussis into a loop near '
                               'the catalytic active site of the thermostable '
                               'alcohol dehydrogenase D from Pyrococcus furiosus. '
                               'The resultant chimera, beta-AdhD, gains the '
                               'calcium-binding ability of the beta-roll, retains '
                               'the thermostable activity of AdhD, and exhibits '
                               'reduced overall alcohol dehydrogenase activity. '
                               'The addition of calcium to beta-AdhD '
                               'preferentially inhibits NAD+-dependent activity in '
                               'comparison to NADP+-dependent activity. Calcium is '
                               'a competitive inhibitor of AdhD, and the addition '
                               'of the RTX domain introduces calcium-dependent '
                               'noncompetitive inhibition to beta-AdhD affecting '
                               'NAD+-dependent activity <289>',
                    'data': 'NAD+',
                    'refs': [1,
                             2,
                             3,
                             4,
                             5,
                             6,
                             7,
                             8,
                             9,
                             10,
                             11,
                             12,
                             13,
                             14,
                             15,
                             16,
                             17,
                             18,
                             19,
                             20,
                             21,
                             22,
                             23,
                             24,
                             25,
                             26,
                             27,
                             28,
                             29,
                             30,
                             31,
                             32,
                             33,
                             34,
                             35,
                             36,
                             37,
                             38,
                             39,
                             40,
                             41,
                             42,
                             43,
                             44,
                             45,
                             46,
                             47,
                             48,
                             49,
                             50,
                             51,
                             52,
                             53,
                             54,
                             55,
                             56,
                             57,
                             58,
                             59,
                             60,
                             61,
                             62,
                             63,
                             64,
                             65,
                             66,
                             67,
                             68,
                             69,
                             70,
                             71,
                             72,
                             73,
                             74,
                             75,
                             76,
                             77,
                             78,
                             79,
                             80,
                             81,
                             82,
                             83,
                             84,
                             85,
                             86,
                             87,
                             88,
                             89,
                             90,
                             91,
                             92,
                             93,
                             94,
                             95,
                             96,
                             97,
                             98,
                             99,
                             100,
                             101,
                             102,
                             103,
                             105,
                             110,
                             111,
                             112,
                             113,
                             114,
                             115,
                             116,
                             118,
                             120,
                             121,
                             124,
                             125,
                             126,
                             127,
                             128,
                             129,
                             130,
                             135,
                             136,
                             137,
                             138,
                             139,
                             141,
                             143,
                             144,
                             146,
                             148,
                             149,
                             152,
                             153,
                             154,
                             156,
                             157,
                             158,
                             159,
                             161,
                             162,
                             163,
                             164,
                             165,
                             169,
                             172,
                             180,
                             194,
                             195,
                             196,
                             197,
                             198,
                             200,
                             201,
                             202,
                             203,
                             204,
                             205,
                             206,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             215,
                             217,
                             218,
                             219,
                             220,
                             221,
                             222,
                             223,
                             225,
                             226,
                             227,
                             229,
                             230,
                             231,
                             232,
                             233,
                             234,
                             237,
                             243,
                             252,
                             254,
                             256,
                             257,
                             260,
                             269,
                             272,
                             279,
                             286,
                             287,
                             288,
                             289,
                             290,
                             292,
                             293]}]),
                 ('ID', '1.1.1.1'),
                 ('IN',
                  [{'comment': '#100# 50% (v/v), 29% loss of activity <173>; #107# '
                               'DMSO inhibits isozyme ADH2-catalysed oxidation in '
                               'an uncompetitive mode and reduction in a mixed '
                               'mode <214>; #107# DMSO inhibits isozymes '
                               'ADH1C-catalysed oxidation in an uncompetitive mode '
                               'and reduction in a mixed mode, no inhibition is '
                               'detected with isozyme ADH3 <214>; #110# DMSO '
                               'inhibits isozymes ADH4-catalysed oxidation in an '
                               'uncompetitive mode and reduction in a mixed mode '
                               '<214>',
                    'data': 'DMSO',
                    'refs': [173, 214]},
                   {'comment': '#46# competitive inhibitor <163>; #8# 1 mM, 31% '
                               'inhibition <23>; #8# class III enzyme is '
                               'completely insensitive to inhibition <11,16>; #8# '
                               'poor inhibitor, class II isoenzyme <14>; #8# no '
                               'inhibition by 12 mM <21>; #8# competitive against '
                               'ethanol <96>; #36# isoenzyme AA-ADH, BB-ADH and '
                               'TT-ADH <95>; #5# inhibits cell protein '
                               'carbonylation following exposure to crotyl alcohol '
                               '<117>',
                    'data': '4-Methylpyrazole',
                    'refs': [2,
                             11,
                             14,
                             16,
                             21,
                             23,
                             24,
                             25,
                             95,
                             96,
                             117,
                             135,
                             163,
                             214]},
                   {'comment': '#91# substrate inhibition above 0.5 M <105>; #100# '
                               '50% (v/v), 59% loss of activity <173>; #107# '
                               'ethanol competitively inhibits the oxidation of '
                               '1-hydroxymethylpyrene by ADH1C and ADH3 <214>; '
                               '#110# ethanol competitively inhibits the oxidation '
                               'of 1-hydroxymethylpyrene by ADH4 <214>',
                    'data': 'ethanol',
                    'refs': [105, 173, 214]}]),
                 ('KI',
                  [{'chebi': 'CHEBI:16236',
                    'comment': '#110# isozyme ADH4, using 1-hydroxymethylpyrene as '
                               'substrate <214>',
                    'data': '3.3 {ethanol}',
                    'refs': [214],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 3.3}]),
                 ('KM',
                  [{'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.000035 {1-formyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 3.5e-05},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.000036 {1-formyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-formyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 3.6e-05},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.00028 {1-hydroxymethyl-6-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-6-methylpyrene',
                    'units': 'mM',
                    'value': 0.00028},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.00048 {4-formylpyrene}',
                    'refs': [214],
                    'substrate': '4-formylpyrene',
                    'units': 'mM',
                    'value': 0.00048},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.00092 {1-formylpyrene}',
                    'refs': [214],
                    'substrate': '1-formylpyrene',
                    'units': 'mM',
                    'value': 0.00092},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.0016 {1-hydroxymethyl-8-methylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethyl-8-methylpyrene',
                    'units': 'mM',
                    'value': 0.0016},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.0029 {4-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '4-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.0029},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.0069 {2-formylpyrene}',
                    'refs': [214],
                    'substrate': '2-formylpyrene',
                    'units': 'mM',
                    'value': 0.0069},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.0283 {1-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '1-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.0283},
                   {'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '0.033 {2-hydroxymethylpyrene}',
                    'refs': [214],
                    'substrate': '2-hydroxymethylpyrene',
                    'units': 'mM',
                    'value': 0.033},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '12.7 {acetaldehyde}',
                    'refs': [214],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 12.7},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#110# isozyme ADH4, at 21-23°C <214>',
                    'data': '3.6 {ethanol}',
                    'refs': [214],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 3.6}]),
                 ('LO',
                  [{'comment': '#61# 2 isozymes <113>; #24# enzyme polymer forms '
                               'rod-like helical particles <128>',
                    'data': 'cytosol',
                    'refs': [113, 128, 135, 194, 214]}]),
                 ('MW',
                  [{'comment': '#113# SDS-PAGE <197>; #107# isozyme ADH2, apparent '
                               'molecular weight deduced from electrophoretic '
                               'mobility <214>; #110# isozyme ADH4, calculated '
                               'from amino acid sequence <214>; #93,133# 4 * '
                               '40000, SDS-PAGE <144,239>; #8,10,36,53,80# 2 * '
                               '40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,81,132# '
                               'x * 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, '
                               'ADH-3, SDS-PAGE <49>; #42# 2 * 40000, enzyme form '
                               'ADHI <68>',
                    'data': '40000',
                    'refs': [11,
                             16,
                             23,
                             24,
                             44,
                             49,
                             52,
                             59,
                             68,
                             87,
                             95,
                             144,
                             197,
                             214,
                             227,
                             239,
                             272]},
                   {'comment': '#107# isozyme ADH1C, apparent molecular weight '
                               'deduced from electrophoretic mobility <214>; #110# '
                               'isozyme ADH4, apparent molecular weight deduced '
                               'from electrophoretic mobility <214>',
                    'data': '40500',
                    'refs': [214]}]),
                 ('OSS',
                  [{'comment': '#107,110# DMSO is not an ideal '
                               'substrate-delivering solvent for ADH-catalysed '
                               'reactions <214>; #151# 20% v/v, 24 h, 87% residual '
                               'activity <244>; #56# 20% v/v, 70% residual '
                               'activity <255>',
                    'data': 'DMSO',
                    'refs': [214, 244, 255]}]),
                 ('RE',
                  {'a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,41# '
                   'ordered bi-bi mechanism <31,43>; #4,76# rapid equilibrium '
                   'random mechanism <63>; #8# ordered bi bi mechanism with '
                   'cofactor adding first to form a binary enzyme complex <23>; '
                   '#41# isoenzyme EE and SS: ordered bi bi mechanism <35>; '
                   '#10,33# mechanism is predominantly ordered with ethanol, but '
                   'partially random with butanol <91>; #41# kinetic mechanism is '
                   'random for ethanol oxidation and compulsory ordered for '
                   'acetaldehyde reduction <41>; #38# oxidizes ethanol in an '
                   'ordered bi-bi mechanism with NAD+ as the first substrate fixed '
                   '<85>; #10# compulsory-order mechanism with the rate-limiting '
                   'step being the dissociation of the product enzyme-NAD+ complex '
                   '<90>; #28,68,79# Theorell-Chance mechanism <38,69,74>; #44# '
                   'sequential reaction mechanism <114>; #88# active site '
                   'structure <127>; #79# catalytic mechanism involves a proton '
                   'relay modulated by the coupled ionization of the active site '
                   'Lys155/Tyr151 pair, and a NAD+ ribose 2-OH switch, other '
                   'active site residues are Ser138 and Trp144, ionization '
                   'properties, substrate binding, overview <130>; #8# class IV '
                   'alcohol dehydrogenase also functions as retinol dehydrogenase, '
                   'reaction and kinetic mechanism: asymmetric rapid equilibrium '
                   'random mechanism with 2 dead-end ternary complexes fro retinol '
                   'oxidation and a rapid equilibrium ordered mechanism with one '
                   'dead-end ternary complex for retinal reduction, a unique '
                   'mechanistic form fro zinc-containing ADH in the medium chain '
                   'dehydrogenase/reductase superfamily of enzymes <124>; #10# '
                   'detailed determination of the reaction and kinetic mechanisms, '
                   'active site structure and determination of amino acid residues '
                   'involved in catalysis, 3 isozymes <120>; #117# ordered bibi '
                   'mechanism, structural and functional implications of amino '
                   'acid residue 47 <110>; #41# ordered sequential bibi reaction '
                   'mechanism, modeling of oxidation kinetic mechanism <117>; '
                   '#119# reaction mechanism, His51 is involved, but not '
                   'essential, in catalysis facilitating the deprotonation of the '
                   'hydroxyl group of water or alcohol ligated to the catalytic '
                   'zinc <111>; #8# Ser48 is involved in catalysis, isozyme '
                   'gamma(2)gamma(2) <109>; #27# the catalytic triad consists of '
                   'Cys44, His67, and Cys154, active site structure <129>)',
                   'a secondary alcohol + NAD+ = a ketone + NADH + H+'}),
                 ('RN', {'alcohol dehydrogenase'}),
                 ('RT', {'redox reaction', 'reduction', 'oxidation'}),
                 ('SN', {'alcohol:NAD+ oxidoreductase'}),
                 ('SP',
                  [{'data': '1-hydroxymethyl-6-methylpyrene + NAD+ = '
                            '1-formyl-6-methylpyrene + NADH + H+ {r}',
                    'refs': [214]},
                   {'data': '1-hydroxymethyl-8-methylpyrene + NAD+ = '
                            '1-formyl-8-methylpyrene + NADH + H+ {r}',
                    'refs': [214]},
                   {'data': '1-hydroxymethylpyrene + NAD+ = 1-formylpyrene + NADH '
                            '+ H+ {r}',
                    'refs': [214]},
                   {'data': '2-hydroxymethylpyrene + NAD+ = 2-formylpyrene + NADH '
                            '+ H+ {r}',
                    'refs': [214]},
                   {'data': '4-hydroxymethylpyrene + NAD+ = 4-formylpyrene + NADH '
                            '+ H+ {r}',
                    'refs': [214]},
                   {'comment': '#48# best substrate <223>; #79,112# 100% activity '
                               '<61,213>; #101# no activity with NADP+, in reverse '
                               'reaction no activity with NADPH <171>; #31# the '
                               'enzyme is highly specific for ethanol with NAD+ as '
                               'the coenzyme <181>; #113# 88% activity compared to '
                               'cyclohexanol <197>; #107# substrate for isozyme '
                               'ADH1C, extremely poor substrate for isozyme ADH3 '
                               '<214>; #107# substrate for isozyme ADH2 <214>; '
                               '#110# substrate for isozyme ADH4 <214>; #134# the '
                               'enzyme shows a preference for short-chain alcohols '
                               'ethanol and 1-propanol <237>; #155# 12% of the '
                               'activity with butan-1-ol <271>; #161# 33% of the '
                               'activity with 1,4-butanediol <286>) |#120# 83% of '
                               'the activity with butan-2-ol <256>',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH + H+',
                    'refs': [61,
                             66,
                             79,
                             85,
                             103,
                             136,
                             139,
                             140,
                             143,
                             144,
                             147,
                             148,
                             153,
                             159,
                             161,
                             162,
                             163,
                             171,
                             173,
                             174,
                             181,
                             194,
                             195,
                             196,
                             197,
                             203,
                             205,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             222,
                             223,
                             231,
                             233,
                             237,
                             239,
                             246,
                             252,
                             256,
                             271,
                             277,
                             279,
                             284,
                             286,
                             288]},
                   {'comment': '#48# best substrate <223>; #79,112# 100% activity '
                               '<61,213>; #101# no activity with NADP+, in reverse '
                               'reaction no activity with NADPH <171>; #31# the '
                               'enzyme is highly specific for ethanol with NAD+ as '
                               'the coenzyme <181>; #113# 88% activity compared to '
                               'cyclohexanol <197>; #107# substrate for isozyme '
                               'ADH1C, extremely poor substrate for isozyme ADH3 '
                               '<214>; #107# substrate for isozyme ADH2 <214>; '
                               '#110# substrate for isozyme ADH4 <214>; #134# the '
                               'enzyme shows a preference for short-chain alcohols '
                               'ethanol and 1-propanol <237>; #155# 12% of the '
                               'activity with butan-1-ol <271>; #161# 33% of the '
                               'activity with 1,4-butanediol <286>) |#120# 83% of '
                               'the activity with butan-2-ol <256>| {r',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH + H+',
                    'refs': [61,
                             66,
                             79,
                             85,
                             103,
                             136,
                             139,
                             140,
                             143,
                             144,
                             147,
                             148,
                             153,
                             159,
                             161,
                             162,
                             163,
                             171,
                             173,
                             174,
                             181,
                             194,
                             195,
                             196,
                             197,
                             203,
                             205,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             222,
                             223,
                             231,
                             233,
                             237,
                             239,
                             246,
                             252,
                             256,
                             271,
                             277,
                             279,
                             284,
                             286,
                             288]},
                   {'comment': '#13# broad substrate specificity <126>; #10# '
                               'constitutive enzyme <94>; #42# key enzyme in '
                               'ethanol production <68>; #52# one constitutive '
                               'enzyme, ADH-MI and one inducible enzyme, ADH-MII '
                               '<82>; #53# enzyme may be involved in the '
                               'metabolism of dietary wax esters in salmonid fish '
                               '<59>; #79# the enzyme oxidizes alcohols to '
                               'aldehydes or ketones both for detoxification and '
                               'metabolic purposes <38>; #36# involvement in the '
                               'development of male hamster reproductive system '
                               '<47>; #89# enzyme shows high substrate specificity '
                               'towards primary aliphatic alcohols, no activity '
                               'with 2-butanol, tert-butanol, isoamyl alcohol, '
                               'isobutyl alcohol, 1,6-hexadiol, and mono-, di-, '
                               'and triethanolamine <118>; #91# no activity with '
                               'methanol, 2-propanol, and isoamyl alcohol <105>; '
                               '#10# substrate specificity and stereospecificity, '
                               'substrate binding pocket structure of the 3 '
                               'isozymes, involving Met294, Trp57, and Trp93 '
                               '<120>; #61# substrate specificity of the 2 '
                               'isozmyes with various substrates, overview, '
                               'isozymes are highly specific for the '
                               '(R)-stereoisomers and enantioselctive for the '
                               'R(-)isomers <113>; #106# the enzyme undergoes a '
                               'substantial conformational change in the apo-holo '
                               'transition, accompanied by loop movements at the '
                               'domain interface <108>; #60# alcohol dehydrogenase '
                               'activity may not limit alcohol supply for ester '
                               'production during ripening <146>; #54# Cm-ADH2 '
                               'cannot reduce branched aldehydes <151>; #10# '
                               'effects of pressure on deuterium isotope effects '
                               'of yeast alcohol dehydrogenase using alternative '
                               'substrates <139>; #93# no activity with methanol '
                               '<144>; #94# the enzyme does not act on short-chain '
                               'normal alkyl alcohols, including methanol and '
                               'ethanol <137>; #97# no activity towards methanol, '
                               'ethanol, 1-propanol, triethylene glycol, '
                               'polyethylene glycol 400, polyethylene glycol 1000, '
                               'D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, '
                               'propionaldehyde, butyraldehyde, and valeraldehyde '
                               '<156>; #99# ADH1 preferrs primary alcohols '
                               'containing C3-C8 carbons to secondary alcohols '
                               'such as 2-propanol and 2-butanol. ADH1 possesses '
                               'specific carboxylate ester-forming activity <172>; '
                               '#102# no activity detected with: '
                               'N-benzyl-2-pyrrolidinone, 2-pyrrolidinone, '
                               '3-hexanone, 4-hydroxy-2-butanone, '
                               '(R)-N-benzyl-3-pyrrolidinol, ethanol, '
                               '1,3-propanediol, 1-butanol, 1,4-butanediol, '
                               '1,2,3-butanetriol, 1,2,4-butanetriol, acetol, '
                               '2-phenyl-1-propanol, 3-phenyl-1-propanol, benzyl '
                               'alcohol and glycerol. No activity with NADP+ or '
                               'NADPH <185>; #6# preference for reduction of '
                               'aromatic ketones and alpha-keto esters, and poor '
                               'activity on aromatic alcohols and aldehydes <169>; '
                               '#26# when NADH is replaced with NADPH, the '
                               'reaction rate is reduced by 0.6% <188>; #41# '
                               'activity is severely reduced towards aliphatic '
                               'alcohols of more than 8 carbon atoms for the free '
                               'enzyme, but not so with immobilized HLAD, '
                               'exhibiting an activity towards C22 and C24 '
                               'aliphatic alcohols higher than 50% of the highest '
                               'value, obtained with C8 <204>; #8# differences in '
                               'the activities of total ADH and class I ADH '
                               'isoenzyme between cancer liver tissues and healthy '
                               'hepatocytes may be a factor in ethanol metabolism '
                               'disorders, which can intensify carcinogenesis '
                               '<180>; #113# TADH is a NAD(H)-dependent enzyme and '
                               'shows a very broad substrate spectrum producing '
                               'exclusively the (S)-enantiomer in high '
                               'enantiomeric excess (more than 99%) during '
                               'asymmetric reduction of ketones <197>; #107# '
                               '1-octanal is no substrate for isozyme ADH1C <214>; '
                               '#107# 1-octanal is no substrate for isozyme ADH2 '
                               '<214>; #110# 1-octanal is no substrate for isozyme '
                               'ADH4 <214>; #113# ADH exhibits a clear preference '
                               'for primary alcohols and corresponding aldehydes '
                               'for aliphatic substrates, in the oxidative '
                               'direction activity steeply increases with chain '
                               'length until 1-propanol and then decreases '
                               'slightly again with growing chain length, '
                               'alpha,beta-unsaturated ketones like 3-penten-2-one '
                               'and cyclohexenone are not converted by ADH, almost '
                               'no conversion of methanol (0.2%) and (+)-carvone '
                               '(0.4%) is detected <197>; #122# no activity is '
                               'detected using 1 mM NADP+ <211>; #111# no activity '
                               'towards methanol <210>; #115# substrates are a '
                               'broad range of alkyl alcohols from ethanol to '
                               '1-triacontanol <215>; #124# the physiological '
                               'direction of the catalytic reaction is reduction '
                               'rather than oxidation <219>; #125# the enzyme '
                               'displays a preference for the reduction of '
                               'alicyclic, bicyclic and aromatic ketones and '
                               'alpha-ketoesters, but is poorly active on '
                               'aliphatic, cyclic and aromatic alcohols, showing '
                               'no activity on aldehydes <218>; #124# the enzyme '
                               'shows no activity on aliphatic linear and branched '
                               'alcohols, except for a poor activity on '
                               '2-propyn-1-ol, 3-methyl-1-butanol and 2-pentanol; '
                               'however, it shows a discrete activity on aliphatic '
                               'cyclic and bicyclic alcohols. Benzyl alcohol and '
                               '4-bromobenzyl alcohol are not found to be '
                               'substrates. The S and R enantiomers of '
                               'a-(trifluoromethyl)benzyl alcohol and methyl and '
                               'ethyl mandelates show no apparent activity with '
                               'SaADH. The enzyme shows poor activity on '
                               '(+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol '
                               'and the two enantiomers of 1-(2-naphthyl)ethanol. '
                               'The enzyme is not active on aliphatic and aromatic '
                               'aldehydes, and on aliphatic linear, branched and '
                               'cyclic ketones except for 3-methylcyclohexanone. '
                               'Catalytic inactivity is observed with acetophenone '
                               'and (S)-a-(trifluoromethyl)benzyl <219>; #128# '
                               'methanol, formaldehyde, and acetone are no '
                               'substrates for HpADH3 <222>; #48# no activity with '
                               'methanol, 1-butanol, glycerol or 2-propanol <223>; '
                               '#129# substrate specificity and '
                               'enantiospecificity, overview. The (R)-specific '
                               'alcohol dehydrogenase requires NADH and reduces '
                               'various kinds of carbonyl compounds, including '
                               'ketones and aldehydes. AFPDH reduces '
                               'acetylpyridine derivatives, beta-keto esters, and '
                               'some ketones compounds with high '
                               'enantiospecificity, overview. No activity with '
                               '2-chlorobenzaldehyde and 2-tetralone, poor '
                               'activity with 1-tetralone, pyruvate, '
                               '2-oxobutyrate, oxalacetate, cyclopentanone, '
                               'cyclohexanone, cycloheptanone, and dipropylketone. '
                               'No activity with 1,2-propanediol, '
                               '3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol, '
                               'glycerol, 1-pentanol, poor activity with '
                               '1-butanol, 1-propanol, ethanol, and methanol '
                               '<225>; #86# the enzyme exhibits broad substrate '
                               'specificity towards aliphatic ketones, '
                               'cycloalkanones, aromatic ketones, and ketoesters '
                               '<226>; #133# the enzyme shows broad substrate '
                               'specificity and prefers aliphatic alcohols and '
                               'ketones. There are no large differences in the '
                               'reactivities between primary and secondary '
                               'alcohols. The enzyme produces (S)-alcohols from '
                               'the corresponding ketones. The values of the '
                               'enantiomeric excess increase with the increase of '
                               'chain length except for the reduction of '
                               '2-hexanone. The highest enantioselectivity is '
                               'shown with the reduction of 2-nonanone <239>; '
                               '#134# the NAD+-dependent HvADH1 shows a preference '
                               'for short-chain alcohols, no activity with '
                               'methanol <237>; #144# broad substrate specificity '
                               'with a preference for the reduction of ketones and '
                               'the oxidation of secondary alcohols <138>; #125# '
                               'enzyme displays a preference for the reduction of '
                               'alicyclic, bicyclic and aromatic ketones and '
                               'alpha-keto esters, but is poorly active on '
                               'aliphatic, cyclic and aromatic alcohols, and shows '
                               'no activity on aldehydes <219>; #150# enzyme '
                               'reduces aldehydes to (R)-alcohols with more than '
                               '99.8% enantiomeric excess <243>; #151# enzyme '
                               'selectively reduces the C=O bond of allylic '
                               'aldehydes/ketones to the corresponding '
                               'alpha,beta-unsaturated alcohols and also has the '
                               'capacity of stereoselectively reducing aromatic '
                               'ketones to (S)-enantioselective alcohols. The '
                               'enzyme preferentially catalyzes oxidation of '
                               'allylic/benzyl aldehydes <244>; #71# ethanol '
                               'dehydrogenase activity of Thermoanaerobium brockii '
                               'is both NAD and NADP linked, reversible, and not '
                               'inhibited by low levels of reaction products '
                               '<103>; #120,143# mutation at the substrate-binding '
                               'site, or at a dimer interface, alters kinetic '
                               'properties and protein oligomeric structure, '
                               'active site flexibility is correlated with subunit '
                               'interactions 20 A away <260>; #6# the enzyme '
                               'transfers the pro-S hydrogen of [4R-(2)H]NADH and '
                               'exhibits Prelog specificity <269>; #41# acycloNAD+ '
                               'i.e. NAD+-analogue, where the nicotinamide ribosyl '
                               'moiety has been replaced by the nicotinamide '
                               '(2-hydroxyethoxy)methyl moiety. There is no '
                               'detectable reduction of acycloNAD+ by secondary '
                               'alcohols although these alcohols serve as '
                               'competitive inhibitors. AcycloNAD+ converts horse '
                               'liver ADH from a broad spectrum alcohol '
                               'dehydrogenase, capable of utilizing either primary '
                               'or secondary alcohols, into an exclusively primary '
                               'alcohol dehydrogenase <275>; #51# bifunctional '
                               'enzyme consisting of an N-terminal acetaldehyde '
                               'dehydrogenase (ALDH) and a C-terminal alcohol '
                               'dehydrogenase (ADH). The specificity constant '
                               '(kcat/Km) is 47fold higher for acetaldehyde '
                               'reductase than that for ethanol dehydrogenase '
                               '<279>; #153# enzyme is an alcohol dehydrogenase '
                               'with additional activity for all-trans-retinol, '
                               'reaction of EC 1.1.1.184 <272>; #155# enzyme shows '
                               'activity as a reductase specific for (S)-acetoin, '
                               'EC 1.1.1.76, and both diacetyl reductase (EC '
                               '1.1.1.304) and NAD+-dependent alcohol '
                               'dehydrogenase (EC 1.1.1.1) activities <271>; #160# '
                               'the enzyme additionally catalyzes selective '
                               'reduction of 3-quinuclidinone to '
                               '(R)-3-quinuclidinol, with 84% ee and 62% '
                               'conversion after 22 h <274>; #162# Candida '
                               'albicans ADH1 is a bifunctional enzyme that '
                               'catalyzes methylglyoxal oxidation and reduction, '
                               'cf. EC 1.2.1.23 <287>; #161# the enzyme catalyzes '
                               'NAD(H)-dependent oxidation of various alcohols and '
                               'reduction of aldehydes, with a marked preference '
                               'for substrates with functional group at the '
                               'terminal carbon atom <286>; #166# almost no '
                               'activity with D-arabinonate, D-lyxonate, '
                               'D-galactonate, glycerol, meso-erythritol, '
                               'D-ribitol, D-arabitol, D-xylitol, and D-mannitol. '
                               'No activity with propanal, butanal, hexanal, and '
                               '4-oxobutanoic acid <292>; #165# the enzyme '
                               'catalyzes the reduction of acetophenone '
                               'derivatives to the corresponding (S)-chiral '
                               'alcohols in an enantiomerically pure form. The '
                               'substituents on the benzene ring of the aryl '
                               'ketones exert some effect on the enzyme activity, '
                               'although the influence is not dramatic. The '
                               'enantioselectivity of the reduction is not '
                               'affected by the substituents and pattern of the '
                               'substitution. The alpha-chlorinated acetophenone '
                               'shows a much higher activity than the '
                               'unsubstituted one (more than 10 times) <294>',
                    'data': 'more = ?',
                    'refs': [38,
                             47,
                             59,
                             68,
                             82,
                             94,
                             103,
                             105,
                             108,
                             113,
                             118,
                             120,
                             126,
                             137,
                             138,
                             139,
                             144,
                             146,
                             151,
                             156,
                             169,
                             172,
                             180,
                             185,
                             188,
                             197,
                             204,
                             210,
                             211,
                             214,
                             215,
                             218,
                             219,
                             222,
                             223,
                             225,
                             226,
                             237,
                             239,
                             243,
                             244,
                             260,
                             269,
                             271,
                             272,
                             274,
                             275,
                             279,
                             286,
                             287,
                             292,
                             294]}]),
                 ('ST',
                  [{'bto': 'BTO:0003833',
                    'comment': '#107,110# isozyme ADH4 <214>',
                    'data': 'buccal mucosa',
                    'refs': [214]}]),
                 ('SY',
                  [{'comment': '#110# isozyme <214>',
                    'data': 'ADH4',
                    'refs': [124, 174, 177, 214, 252]}]),
                 ('references',
                  {1: {'info': 'Talbot, B.G.; Qureshi, A.A.; Cohen, R.; Thirion, '
                               'J.P.: Purification and properties of two distinct '
                               'groups of ADH isozymes from Chinese hamster liver. '
                               'Biochem. Genet. (1981) 19, 813-829.',
                       'pubmed': 6794566},
                   2: {'info': 'Fong, W.P.: Isolation and characterization of '
                               'grass carp (Ctenopharyngodon idellus) liver '
                               'alcohol dehydrogenase. Comp. Biochem. Physiol. B '
                               '(1991) 98, 297-302.'},
                   3: {'info': 'Pessione, E.; Pergola, L.; Cavaletto, M.; Giunta, '
                               'C.; Trotta, A.; Vanni, A.: Extraction, '
                               'purification and characterization of ADH1 from the '
                               'budding yeast Kluyveromyces marxianus. Ital. J. '
                               'Biochem. (1990) 39, 71-82.',
                       'pubmed': 2193901},
                   4: {'info': 'Leblova, S.; El Ahmad, M.: Characterization of '
                               'alcohol dehydrogenase isolated from germinating '
                               'bean (Vicia faba) seeds. Collect. Czech. Chem. '
                               'Commun. (1989) 54, 2519-2527.'},
                   5: {'info': 'Keung, W.M.; Ho, Y.W.; Fong, W.P.; Lee, C.Y.: '
                               'Isolation and characterization of shrew (Suncus '
                               'murinus) liver alcohol dehydrogenase. Comp. '
                               'Biochem. Physiol. B (1989) 93, 169-173.',
                       'pubmed': 2666017},
                   6: {'info': 'Tong, W.F.; Lin, S.W.: Purification and '
                               'biochemical properties of rice alcohol '
                               'dehydrogenase. Bot. Bull. Acad. Sin. (1988) 29, '
                               '245-253.'},
                   7: {'info': 'Van Geyt, J.; Jacobs, M.; Triest, L.: '
                               'Characterization of alcohol dehydrogenase in Najas '
                               'marina L. Aquat. Bot. (1987) 28, 129-141.'},
                   8: {'info': 'Vilageliu, L.; Juan, E.; Gonzalez-Duarte, R.: '
                               'Determination of some biochemical features of '
                               'alcohol dehydrogenase from Drosophila '
                               'melanogaster, Drosophila simulans, Drosophila '
                               'virilis, Drosophila funebris, Drosophila imigrans '
                               'and drosophila lebanonensis. Comparison of their '
                               'properties and estimation of the homology of the '
                               'ADH enzyme of different species. Adv. Genet. , '
                               'Dev. , Evol. Drosophila, [Proc. Eur. Drosophila '
                               'Res. Conf. ] (Lakovaara, S. , ed. ) Plenum N. Y. '
                               '(1982) 7, 237-250.'},
                   9: {'info': 'Edenberg, H.J.; Brown, C.J.; Carr, L.G.; Ho, W.H.; '
                               'Hu, M.W.: Alcohol dehydrogenase gene expression '
                               'and cloning of the mouse chi-like ADH. Adv. Exp. '
                               'Med. Biol. (1991) 284, 253-262.',
                       'pubmed': 2053480},
                   10: {'info': 'Herrera, E.; Zorzano, A.; Fresneda, V.: '
                                'Comparative kinetics of human and rat liver '
                                'alcohol dehydrogenase. Biochem. Soc. Trans. '
                                '(1983) 11, 729-730.'},
                   11: {'info': 'Dafeldecker, W.P.; Vallee, B.L.: Organ-specific '
                                'human alcohol dehydrogenase: isolation and '
                                'characterization of isozymes from testis. '
                                'Biochem. Biophys. Res. Commun. (1986) 134, '
                                '1056-1063.',
                        'pubmed': 2936344},
                   12: {'info': 'Woronick, C.L.: Alcohol dehydrogenase from human '
                                'liver. Methods Enzymol. (1975) 41B, 369-374.',
                        'pubmed': 236461},
                   13: {'info': 'Wagner, F.W.; Burger, A.R.; Vallee, B.L.: Kinetic '
                                'properties of human liver alcohol dehydrogenase: '
                                'oxidation of alcohols by class I isoenzymes. '
                                'Biochemistry (1983) 22, 1857-1863.',
                        'pubmed': 6342669},
                   14: {'info': 'Ditlow, C.C.; Holmquist, B.; Morelock, M.M.; '
                                'Vallee, B.L.: Physical and enzymatic properties '
                                'of a class II alcohol dehydrogenase isozyme of '
                                'human liver: pi-ADH. Biochemistry (1984) 23, '
                                '6363-6368.',
                        'pubmed': 6397223},
                   15: {'info': 'Yin, S.J.; Bosron, W.F.; Magnes, L.J.; Li, T.K.: '
                                'Human liver alcohol dehydrogenase: purification '
                                'and kinetic characterization of the beta 2 beta '
                                '2, beta 2 beta 1, alpha beta 2, and beta 2 gamma '
                                '1 Oriental isoenzymes. Biochemistry (1984) 23, '
                                '5847-5853.',
                        'pubmed': 6395883},
                   16: {'info': 'Wagner, F.W.; Pares, X.; Holmquist, B.; Vallee, '
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                 ('tissues', {'BTO:0003833'})])
    ──────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────────
    OrderedDict([('protein_id', 8),
                 ('ec', '1.1.1.1'),
                 ('organism', 'Homo sapiens'),
                 ('taxonomy', 9606),
                 ('uniprot', None),
                 ('AP',
                  [{'comment': '#24# isozyme ADH2 is a target for anti-amoebic '
                               'agents <123>; #8# organ simulations indicate that '
                               'higher therapeutic acetaminophen (0.5 mM) inhibits '
                               '16% of allotype ADH1B*1/*1 hepatic ADH activity at '
                               '2-20 mM ethanol and that therapeutic salicylate '
                               '(1.5 mM) inhibits 30-31% of the allotype '
                               'ADH1B*2/*2 activity, suggesting potential '
                               'significant inhibitions of ethanol first-pass '
                               'metabolism in these allelotypes <273>',
                    'data': 'medicine',
                    'refs': [123, 273]}]),
                 ('CF',
                  [{'comment': '#13,24,44,61,111,113,166# dependent on '
                               '<113,114,126,128,197,210,292>; #122# specific for '
                               'NAD+ <211>; #162# specific for <287>; #46,96# '
                               'dependent <153,154,159>; #163# preferred cofactor '
                               '<288>; #41# kinetics of coenzyme binding in the '
                               'pH-range 10-12 <26>; #4# NAD+-plus-acetone-induced '
                               'conversion <62>; #41# NAD+ acts as an activator '
                               'which induces an active form of the enzyme <34>; '
                               '#41# preferred substrate <42>; #85# activity with '
                               'mutants G223D/T224I and G223D/T224I/H225N <125>; '
                               '#10# cofactor binding mode <120>; #120# dependent '
                               'on, cofactor binding mechanism and conformation '
                               'from crystal structure analysis <112>; #88# the '
                               'monomer consists of a catalytic and a '
                               'cofactor-binding domain, the cofactor is bound '
                               'between 2 domains in a cleft <127>; '
                               '#7,27,34,50,66# strongly preferred as cofactor '
                               '<135>; #93# specific for NAD+, no activity with '
                               'NADP+, pro-R stereospecificity for hydrogen '
                               'transfer <144>; #99# ADH1 preferrs NAD+ 205fold '
                               'better than NADP+ as cofactor <172>; #15# ADH3 '
                               'does not react with NADP+ <172>; #144# preferred '
                               'over NADP+ <138>; #6# strict requirement for '
                               'NAD(H) as the coenzyme. Critical role of the D37 '
                               'residue in discriminating NAD(H) from NADP(H) '
                               '<169>; #112# shows NAD+ as the preferred co-factor '
                               'over NADP+ <213>; #41# the binding of NAD+ is '
                               'kinetically limited by a unimolecular '
                               'isomerization (corresponding to the conformational '
                               'change) that is controlled by deprotonation of the '
                               'catalytic zinc-water to produce a '
                               'negatively-charged zinc-hydroxide, which can '
                               'attract the positively-charged nicotinamide ring '
                               '<198>; #115# NAD+ is prefered over NADP+ <215>; '
                               '#116# NADP+ is prefered over NAD+ <215>; #125# '
                               'strict requirement for NAD(H) as the coenzyme, no '
                               'activity with NADP+. The specificity constant '
                               'value is 6fold higher for NADH than NAD+ <218>; '
                               '#124# the enzyme transfers the deuteride to the '
                               'Si-face of NAD+ <219>; #48# Adh3 is strictly '
                               'dependent on NAD+/NADH, and shows no activity with '
                               'NADP+/NADPH as cofactor <223>; #134# exclusively '
                               'NAD+ dependent <237>; #51# 57fold preferred over '
                               'NADP+ <279>; #23# H255R single mutant exhibits an '
                               'increased binding affinity toward NADP+ and a '
                               'concomitant reduction in affinity for NAD+ <290>; '
                               '#23# insertion of an RTX domain from the adenylate '
                               'cyclase of Bordetella pertussis into a loop near '
                               'the catalytic active site of the thermostable '
                               'alcohol dehydrogenase D from Pyrococcus furiosus. '
                               'The resultant chimera, beta-AdhD, gains the '
                               'calcium-binding ability of the beta-roll, retains '
                               'the thermostable activity of AdhD, and exhibits '
                               'reduced overall alcohol dehydrogenase activity. '
                               'The addition of calcium to beta-AdhD '
                               'preferentially inhibits NAD+-dependent activity in '
                               'comparison to NADP+-dependent activity. Calcium is '
                               'a competitive inhibitor of AdhD, and the addition '
                               'of the RTX domain introduces calcium-dependent '
                               'noncompetitive inhibition to beta-AdhD affecting '
                               'NAD+-dependent activity <289>',
                    'data': 'NAD+',
                    'refs': [1,
                             2,
                             3,
                             4,
                             5,
                             6,
                             7,
                             8,
                             9,
                             10,
                             11,
                             12,
                             13,
                             14,
                             15,
                             16,
                             17,
                             18,
                             19,
                             20,
                             21,
                             22,
                             23,
                             24,
                             25,
                             26,
                             27,
                             28,
                             29,
                             30,
                             31,
                             32,
                             33,
                             34,
                             35,
                             36,
                             37,
                             38,
                             39,
                             40,
                             41,
                             42,
                             43,
                             44,
                             45,
                             46,
                             47,
                             48,
                             49,
                             50,
                             51,
                             52,
                             53,
                             54,
                             55,
                             56,
                             57,
                             58,
                             59,
                             60,
                             61,
                             62,
                             63,
                             64,
                             65,
                             66,
                             67,
                             68,
                             69,
                             70,
                             71,
                             72,
                             73,
                             74,
                             75,
                             76,
                             77,
                             78,
                             79,
                             80,
                             81,
                             82,
                             83,
                             84,
                             85,
                             86,
                             87,
                             88,
                             89,
                             90,
                             91,
                             92,
                             93,
                             94,
                             95,
                             96,
                             97,
                             98,
                             99,
                             100,
                             101,
                             102,
                             103,
                             105,
                             110,
                             111,
                             112,
                             113,
                             114,
                             115,
                             116,
                             118,
                             120,
                             121,
                             124,
                             125,
                             126,
                             127,
                             128,
                             129,
                             130,
                             135,
                             136,
                             137,
                             138,
                             139,
                             141,
                             143,
                             144,
                             146,
                             148,
                             149,
                             152,
                             153,
                             154,
                             156,
                             157,
                             158,
                             159,
                             161,
                             162,
                             163,
                             164,
                             165,
                             169,
                             172,
                             180,
                             194,
                             195,
                             196,
                             197,
                             198,
                             200,
                             201,
                             202,
                             203,
                             204,
                             205,
                             206,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             215,
                             217,
                             218,
                             219,
                             220,
                             221,
                             222,
                             223,
                             225,
                             226,
                             227,
                             229,
                             230,
                             231,
                             232,
                             233,
                             234,
                             237,
                             243,
                             252,
                             254,
                             256,
                             257,
                             260,
                             269,
                             272,
                             279,
                             286,
                             287,
                             288,
                             289,
                             290,
                             292,
                             293]},
                   {'comment': '#129# required <225>; #44,61# dependent on '
                               '<113,114>; #46# dependent <155>; #163# preferred '
                               'cofactor <288>; #41# kinetics of coenzyme binding '
                               'in the pH range 10-12 <26>; #41# preferred '
                               'coenzyme <42>; #85# activity with mutants '
                               'G223D/T224I and G223D/T224I/H225N <125>; #10# '
                               'cofactor binding mode <120>; #125# strictly '
                               'required <219>; #6# strict requirement for NAD(H) '
                               'as the coenzyme. Critical role of the D37 residue '
                               'in discriminating NAD(H) from NADP(H) <169>; #125# '
                               'strict requirement for NAD(H) as the coenzyme, no '
                               'activity with NADPH. The specificity constant '
                               'value is 6fold higher for NADH than NAD+ <218>; '
                               '#124# the specificity constant value is 21-fold '
                               'higher for NADH than NAD+. No activity with '
                               'NADP(H) <219>; #48# Adh3 is strictly dependent on '
                               'NAD+/NADH, and shows no activity with NADP+/NADPH '
                               'as cofactor <223>; #6# the enzyme transfers the '
                               'pro-S hydrogen of [4R-(2)H]NADH and exhibits '
                               'Prelog specificity <269>; #164# the cofactor NADH '
                               'can be recycled with D-glucose '
                               'dehydrogenase/D-glucose system or in a coupled '
                               'substrate approach using isopropanol as the '
                               'hydrogen donor <291>',
                    'data': 'NADH',
                    'refs': [1,
                             2,
                             3,
                             4,
                             5,
                             6,
                             7,
                             8,
                             9,
                             10,
                             11,
                             12,
                             13,
                             14,
                             15,
                             16,
                             17,
                             18,
                             19,
                             20,
                             21,
                             22,
                             23,
                             24,
                             25,
                             26,
                             27,
                             28,
                             29,
                             30,
                             31,
                             32,
                             33,
                             34,
                             35,
                             36,
                             37,
                             38,
                             39,
                             40,
                             41,
                             42,
                             43,
                             44,
                             45,
                             46,
                             47,
                             48,
                             49,
                             50,
                             51,
                             52,
                             53,
                             54,
                             55,
                             56,
                             57,
                             58,
                             59,
                             60,
                             61,
                             62,
                             63,
                             64,
                             65,
                             66,
                             67,
                             68,
                             69,
                             70,
                             71,
                             72,
                             73,
                             74,
                             75,
                             76,
                             77,
                             78,
                             79,
                             80,
                             81,
                             82,
                             83,
                             84,
                             85,
                             86,
                             87,
                             88,
                             89,
                             90,
                             91,
                             92,
                             93,
                             94,
                             95,
                             96,
                             97,
                             98,
                             99,
                             100,
                             101,
                             102,
                             105,
                             110,
                             113,
                             114,
                             118,
                             120,
                             123,
                             124,
                             125,
                             129,
                             131,
                             132,
                             133,
                             134,
                             137,
                             140,
                             149,
                             151,
                             155,
                             157,
                             158,
                             161,
                             163,
                             169,
                             200,
                             215,
                             217,
                             218,
                             219,
                             222,
                             223,
                             225,
                             226,
                             231,
                             232,
                             233,
                             234,
                             241,
                             246,
                             252,
                             253,
                             256,
                             259,
                             265,
                             269,
                             272,
                             281,
                             285,
                             286,
                             287,
                             288,
                             290,
                             291]}]),
                 ('CL',
                  [{'data': '(5-7 genes encoding ADH, DNA and amino acid sequence '
                            'determination and analysis, polymorphism and allelic '
                            'frequencies analysis, gene ADH2 possesses 2 allelic '
                            'forms with Ile308 or Val308, expression of ADH2 '
                            'alloenzymes in Escherichia coli)',
                    'refs': [115]},
                   {'data': '(class IV enzyme, expression in Escherichia coli)',
                    'refs': [53]},
                   {'data': '(expression of ADH1C*2 in Escherichia coli)',
                    'refs': [116]},
                   {'data': '(expression of ADH4 in Escherichia coli)',
                    'refs': [124]},
                   {'data': '(expression of human ADH1 in an in vitro '
                            'transcription/translation system, N-terminally '
                            'GST-tagged ADH1 in COS cells and in Escherichia coli)',
                    'refs': [228]},
                   {'data': '(expression of isozymes in Escherichia coli strain '
                            'BL21)',
                    'refs': [119]}]),
                 ('CR',
                  [{'data': '(isozyme alphaalpha in complex with inhibitor '
                            'N-cyclopentyl-N-cyclobutylformamide, isozyme '
                            'beta(1)beta(1) in complex with inhibitors '
                            'N-benzylformamide and N-heptylformamide, and isozyme '
                            'gamma(2)gamma(2) in complex with inhibitor '
                            'N-1-methylheptylformamide, X-ray diffraction '
                            'structure determination and analysis at 1.45-2.5 A '
                            'resolution, structure modeling)',
                    'refs': [109]},
                   {'data': '', 'refs': [12]}]),
                 ('EN',
                  [{'comment': '#8# isozyme alphaalpha, altered active site '
                               'structure and inhibitor binding <109>',
                    'data': 'A93F',
                    'refs': [109]},
                   {'comment': '#8# isozyme gamma(2)gamma(2), altered active site '
                               'structure and inhibitor binding <109>',
                    'data': 'S48T',
                    'refs': [109]},
                   {'comment': '#8# isozyme gamma(2)gamma(2), altered active site '
                               'structure and inhibitor binding <109>',
                    'data': 'V141L',
                    'refs': [109]}]),
                 ('GS',
                  [{'data': '(100fold purified enzyme is destroyed by freezing)',
                    'refs': [12]}]),
                 ('ID', '1.1.1.1'),
                 ('IN',
                  [{'comment': '#46# competitive inhibitor <163>; #8# 1 mM, 31% '
                               'inhibition <23>; #8# class III enzyme is '
                               'completely insensitive to inhibition <11,16>; #8# '
                               'poor inhibitor, class II isoenzyme <14>; #8# no '
                               'inhibition by 12 mM <21>; #8# competitive against '
                               'ethanol <96>; #36# isoenzyme AA-ADH, BB-ADH and '
                               'TT-ADH <95>; #5# inhibits cell protein '
                               'carbonylation following exposure to crotyl alcohol '
                               '<117>',
                    'data': '4-Methylpyrazole',
                    'refs': [2,
                             11,
                             14,
                             16,
                             21,
                             23,
                             24,
                             25,
                             95,
                             96,
                             117,
                             135,
                             163,
                             214]},
                   {'comment': '#102# 1 mM, complete inhibition <185>; #36# mixed '
                               'type inhibition <47>; #93# 1 mM, 38% inhibition '
                               '<144>; #5# inhibition of isoenzyme A2 and C2, no '
                               'inhibition of isoenzyme B2 <48>; #42# 0.2 mM, '
                               'strong inhibition <68>; #26# 1 mM, 6% inhibition '
                               '<188>',
                    'data': '1,10-phenanthroline',
                    'refs': [2,
                             14,
                             21,
                             24,
                             25,
                             45,
                             47,
                             48,
                             68,
                             69,
                             75,
                             95,
                             144,
                             185,
                             188]},
                   {'comment': '#79# competitive <38>; #89# strong inhibition '
                               '<118>; #8# 0.05 mM, 50% inhibition <10>; #46# '
                               'competitive inhibitor <163>; #79# competitive '
                               'towards ethanol <61>; #9# 0.1-10 mM, ADH-2 is '
                               'practically insensitive, ADH-3 is very sensitive '
                               '<49>; #9# 0.05 mM, complete inhibition <10>; #8# '
                               'no inhibition at 1.0 mM <23>; #43,80# organism has '
                               'a pyrazole-sensitive isoenzyme and a '
                               'pyrazole-insensitive enzyme <24,25>; #69# '
                               'pyrazole-sensitive enzyme forms ADH-1, ADH-2, '
                               'ADH-3 and the pyrazole-insensitive form ADH-An '
                               '<60>; #5# inhibition of isoenzyme A2 and C2. '
                               'Isoenzyme B2 is insensitive to pyrazole inhibition '
                               'with trans-2-hexen-1-ol as substrate <48>',
                    'data': 'pyrazole',
                    'refs': [10,
                             12,
                             23,
                             24,
                             25,
                             38,
                             45,
                             48,
                             49,
                             60,
                             61,
                             71,
                             94,
                             118,
                             163,
                             212]},
                   {'comment': '#8# dead-end inhibitor to the enzyme-cofactor '
                               'complex, inhibition of oxidation reaction <116>',
                    'data': '3-butylthiolan 1-oxide',
                    'refs': [116]},
                   {'comment': '#8# competitive against substrate cyclohexanone '
                               '<116>',
                    'data': '4-androsten-3,17-dione',
                    'refs': [116]},
                   {'data': '4-bromopyrazole', 'refs': [23]},
                   {'data': '4-cyanopyrazole', 'refs': [23]},
                   {'data': '4-nitropyrazole', 'refs': [23]},
                   {'data': '4-octylpyrazole', 'refs': [12]},
                   {'data': '4-pentylpyrazole', 'refs': [12, 23]},
                   {'data': '4-propylpyrazole', 'refs': [23]},
                   {'comment': '#8# i.e. 5alpha-dihydrotestosterone, allosteric, '
                               'competitive against substrate cyclohexanone, '
                               'noncompetitive against NAD+ nd ethanol <116>',
                    'data': '5alpha-androstan-17beta-ol-3-one',
                    'refs': [116]},
                   {'data': '8-Amino-6-methoxyquinoline', 'refs': [12]},
                   {'comment': '#8# 1 mM, 4.4% inhibition of hepatic allotype '
                               'ADH1B*1/*1 activity, 2.8% inhibition of hepatic '
                               'allotype ADH1B*2/*2 activity <273>',
                    'data': 'Acetylsalicylate',
                    'refs': [273]},
                   {'comment': '#8# inhibits isozyme gamma(2)gamma(2) <109>',
                    'data': 'N-1-methylheptylformamide',
                    'refs': [109]},
                   {'comment': '#8# inhibits isozyme beta(1)beta(1) <109>',
                    'data': 'N-benzylformamide',
                    'refs': [109]},
                   {'comment': '#8# inhibits isozyme alphaalpha, complex structure '
                               '<109>',
                    'data': 'N-cyclopentyl-N-cyclobutylformamide',
                    'refs': [109]},
                   {'comment': '#8# inhibits isozyme beta(1)beta(1) <109>',
                    'data': 'N-heptylformamide',
                    'refs': [109]},
                   {'data': 'NADP+', 'refs': [21]},
                   {'comment': '#8# 0.5 mM, 16% inhibition of hepatic allotype '
                               'ADH1B*1/*1 activity, 6.1% inhibition of hepatic '
                               'allotype ADH1B*2/*2 activity <273>',
                    'data': 'acetaminophen',
                    'refs': [273]},
                   {'comment': '#8# product inhibition <124>',
                    'data': 'all-trans-retinal',
                    'refs': [124]},
                   {'comment': '#8# weak feedback inhibition <124>',
                    'data': 'all-trans-retinoic acid',
                    'refs': [124]},
                   {'comment': '#8# 0.2 mM, 2.5% inhibition of hepatic allotype '
                               'ADH1B*1/*1 activity, 12% inhibition of hepatic '
                               'allotype ADH1B*2/*2 activity <273>',
                    'data': 'cimetidine',
                    'refs': [273]},
                   {'comment': '#8# 1.5 mM, 12% inhibition of hepatic allotype '
                               'ADH1B*1/*1 activity, 31% inhibition of hepatic '
                               'allotype ADH1B*2/*2 activity <273>',
                    'data': 'salicylate',
                    'refs': [273]},
                   {'data': 'sulfonic acid', 'refs': [21]},
                   {'comment': '#8# competitive against retinol, noncompetitive '
                               'against NAD+ <124>',
                    'data': 'trifluoroethanol',
                    'refs': [91, 124]},
                   {'comment': '#8# competitive, stabilizes the retinoid '
                               'compounds, elevates the Km values of the '
                               'substrates, most effective at 0.1% w/v <107>; '
                               '#100# 10% (w/v), 89% inhibition <173>; #113# 13% '
                               'relative activity at 10% (v/v) <197>',
                    'data': 'Tween 80',
                    'refs': [107, 173, 197]},
                   {'comment': '#8# substrate inhibition, competitive against '
                               'retinol, noncompetitive against NADH <124>',
                    'data': 'Isobutyramide',
                    'refs': [124, 175]},
                   {'comment': '#26# 1 mM, 31% inhibition <188>; #46# 15 mM, 85% '
                               'inhibition <66>; #61# 67% inhibition of ADH II at '
                               '5 mM, 45% inhibition of ADH I at 1 mM, '
                               'irreversible inhibition, addition of Mg2+ and Zn2+ '
                               'increase the inhibitory effect <113>; #58# 25% '
                               'inhibition at 10.5 mM, 44% inhibition at 21 mM '
                               '<147>; #57# 31% inhibition at 10.5 mM, 92% '
                               'inhibition at 21 mM <147>; #46# loses 30% of its '
                               'activity immediately on addition of EDTA <163>; '
                               '#113# 2.3% relative activity at 10 mM <197>; #125# '
                               '1 mM, 93% of initial activity <219>',
                    'data': 'EDTA',
                    'refs': [14,
                             24,
                             25,
                             66,
                             76,
                             99,
                             113,
                             147,
                             163,
                             188,
                             197,
                             219,
                             223]},
                   {'data': "2,2'-bipyridine", 'refs': [14, 25]},
                   {'comment': '#46# competitive inhibitor <163>',
                    'data': '4-iodopyrazole',
                    'refs': [23, 163]},
                   {'data': '8-hydroxyquinoline 5-sulfonic acid', 'refs': [21, 24]},
                   {'comment': '#118# Zn2+ chelator and inhibitor of ADH <209>',
                    'data': 'dipicolinic acid',
                    'refs': [21, 24, 209]},
                   {'comment': '#36# competitive <47>; #8# 1 mM, 28% inhibition '
                               '<23>; #12# class I ADHs migrate towards cathode on '
                               'starch gel and are very sensitive to '
                               '4-methylpyrazole inhibition, class II ADH migrates '
                               'slowly towards anode and is less sensitive to '
                               '4-methylpyrazole, class II ADH migrates rapidly '
                               'towards anode and is insensitive to '
                               '4-methylpyrazole <46>; #9# 0.1-10 mM, ADH-2 is '
                               'practically insensitive, ADH-3 is very sensitive '
                               '<49>; #9# competitive inhibitor of all four '
                               'isoenzymes <51>',
                    'data': '4-methoxypyrazole',
                    'refs': [23, 45, 46, 47, 49, 51, 53, 91]}]),
                 ('KI',
                  [{'comment': '#8# pH 7.3, 37°C, versus cyclohexanone <116>',
                    'data': '0.0047 {4-androsten-3,17-dione}',
                    'refs': [116],
                    'substrate': '4-androsten-3,17-dione',
                    'units': 'mM',
                    'value': 0.0047},
                   {'comment': '#8# pH 7.3, 37°C, versus cyclohexanone <116>',
                    'data': '0.0047 {5alpha-androstan-17beta-ol-3-one}',
                    'refs': [116],
                    'substrate': '5alpha-androstan-17beta-ol-3-one',
                    'units': 'mM',
                    'value': 0.0047},
                   {'comment': '#8# pH 7.3, 37°C, versus ethanol <116>',
                    'data': '0.014 {5alpha-androstan-17beta-ol-3-one}',
                    'refs': [116],
                    'substrate': '5alpha-androstan-17beta-ol-3-one',
                    'units': 'mM',
                    'value': 0.014},
                   {'comment': '#8# pH 7.3, 37°C, versus NAD+ <116>',
                    'data': '0.028 {5alpha-androstan-17beta-ol-3-one}',
                    'refs': [116],
                    'substrate': '5alpha-androstan-17beta-ol-3-one',
                    'units': 'mM',
                    'value': 0.028},
                   {'comment': '#8# inhibition kinetics <116>',
                    'data': '-999 {more}',
                    'refs': [116, 123, 124],
                    'units': 'mM'}]),
                 ('KM',
                  [{'comment': '#41,71# kinetics <117,121>; #10# pH-dependence of '
                               'Km-value <89>; #4,76# kinetics of ethanol '
                               'oxidation <63>; #41# kinetics of native and '
                               'modified enzyme with coenzyme analogues <54>; #41# '
                               'Km-values of active-site Co(II)substituted enzyme '
                               '<31>; #8# Km values for the class I isoenzymes '
                               'with the substrates ethanol, methanol, ethylene '
                               'glycol, benzyl alcohol, octanol, cyclohexanol and '
                               '16-hydroxyhexadecanoic acid <13>; #8# steady-state '
                               'kinetics <116>; #119# detailed kinetic mechanism, '
                               'steady-state kinetics for wild-type and mutant '
                               'enzymes, investigation of pH-dependency <111>; '
                               '#79# detailed kinetics, computational analysis of '
                               'the reaction mechanism <130>; #5# Km for isozymes '
                               'ADH1, and ADH4 for all retinoid substrates in '
                               'forward and reverse reaction <119>; #8# Km for '
                               'isozymes ADH1B1, ADH1B2, and ADH4 for all retinoid '
                               'substrates in forward and reverse reaction <119>; '
                               '#86,91,163# Michaelis-Menten kinetics '
                               '<105,226,288>; #8# steady-state kinetics, kinetic '
                               'mechanism <124>; #8# steady-state kinetics, MW 25 '
                               'kDa <115>; #10# wild-type and mutant forms of the '
                               '3 isozymes, steady-state kinetics, detailed '
                               'kinetic analysis, at different pH values and '
                               'temperatures <120>; #5# effects of tert-butanol, '
                               'butyramide, valeramide and capronamide on KM-value '
                               'for ethanol <141>; #23# kinetic data füor '
                               'wild-type enzyme and chimeric enzyme created by '
                               'insertion of an RTX domain from the adenylate '
                               'cyclase of Bordetella pertussis into a loop near '
                               'the catalytic active site of the thermostable '
                               'alcohol dehydrogenase D (AdhD) from Pyrococcus '
                               'furiosus <289>',
                    'data': '-999 {more}',
                    'refs': [13,
                             22,
                             23,
                             31,
                             54,
                             63,
                             75,
                             83,
                             89,
                             105,
                             111,
                             115,
                             116,
                             117,
                             119,
                             120,
                             121,
                             124,
                             130,
                             141,
                             226,
                             288,
                             289],
                    'units': 'mM'},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# recombinant allozyme Val308, pH 7.5, 25°C '
                               '<115>',
                    'data': '10.6 {ethanol}',
                    'refs': [115, 135],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 10.6},
                   {'chebi': 'CHEBI:16908',
                    'data': '0.0025 {NADH}',
                    'refs': [16],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 0.0025},
                   {'comment': '#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>',
                    'data': '0.0036 {5alpha-androstan-17beta-ol-3-one}',
                    'refs': [116],
                    'substrate': '5alpha-androstan-17beta-ol-3-one',
                    'units': 'mM',
                    'value': 0.0036},
                   {'comment': '#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>',
                    'data': '0.0036 {5beta-pregnan-3,20-dione}',
                    'refs': [116],
                    'substrate': '5beta-pregnan-3,20-dione',
                    'units': 'mM',
                    'value': 0.0036},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.004 {4-hydroxy-retinol}',
                    'refs': [107],
                    'substrate': '4-hydroxy-retinol',
                    'units': 'mM',
                    'value': 0.004},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme beta1,beta1 <16>',
                    'data': '0.0064 {NADH}',
                    'refs': [16],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 0.0064},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme gamma1,gamma1 <16>',
                    'data': '0.007 {NADH}',
                    'refs': [16],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 0.007},
                   {'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.007 {Octanol}',
                    'refs': [14],
                    'substrate': 'Octanol',
                    'units': 'mM',
                    'value': 0.007},
                   {'chebi': 'CHEBI:17987',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.007 {benzyl alcohol}',
                    'refs': [14],
                    'substrate': 'benzyl alcohol',
                    'units': 'mM',
                    'value': 0.007},
                   {'comment': '#8# isoenzyme beta1,beta1 <17>; #8# isoenzyme '
                               'beta2,beta2 <16>',
                    'data': '0.0074 {NAD+}',
                    'refs': [16, 17],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.0074},
                   {'comment': '#8# isoenzyme gamma1,gamma1 <16,17>',
                    'data': '0.0079 {NAD+}',
                    'refs': [16, 17],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.0079},
                   {'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '0.008 {Cyclohexanol}',
                    'refs': [13],
                    'substrate': 'Cyclohexanol',
                    'units': 'mM',
                    'value': 0.008},
                   {'comment': '#8# isoenzyme gamma2,gamma2 <16,17>',
                    'data': '0.0087 {NAD+}',
                    'refs': [16, 17],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.0087},
                   {'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.009 {Octanol}',
                    'refs': [115],
                    'substrate': 'Octanol',
                    'units': 'mM',
                    'value': 0.009},
                   {'chebi': 'CHEBI:17336',
                    'data': '0.009 {all-trans-retinol}',
                    'refs': [53],
                    'substrate': 'all-trans-retinol',
                    'units': 'mM',
                    'value': 0.009},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.011 {4-hydroxy-retinol}',
                    'refs': [107],
                    'substrate': '4-hydroxy-retinol',
                    'units': 'mM',
                    'value': 0.011},
                   {'chebi': 'CHEBI:78272',
                    'comment': '#8# isozyme ADH1B1, pH 7.5, 25°C <119>',
                    'data': '0.011 {9-cis-retinol}',
                    'refs': [119],
                    'substrate': '9-cis-retinol',
                    'units': 'mM',
                    'value': 0.011},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme alpha,alpha <16>',
                    'data': '0.011 {NADH}',
                    'refs': [16],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 0.011},
                   {'chebi': 'CHEBI:17898',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.011 {all-trans-retinal}',
                    'refs': [107],
                    'substrate': 'all-trans-retinal',
                    'units': 'mM',
                    'value': 0.011},
                   {'chebi': 'CHEBI:50211',
                    'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.011 {retinol}',
                    'refs': [115],
                    'substrate': 'retinol',
                    'units': 'mM',
                    'value': 0.011},
                   {'chebi': 'CHEBI:17898',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.012 {all-trans-retinal}',
                    'refs': [107],
                    'substrate': 'all-trans-retinal',
                    'units': 'mM',
                    'value': 0.012},
                   {'chebi': 'CHEBI:50211',
                    'comment': '#8# recombinant allozyme Val308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.012 {retinol}',
                    'refs': [115],
                    'substrate': 'retinol',
                    'units': 'mM',
                    'value': 0.012},
                   {'comment': '#8# isoenzyme alpha,alpha <16,17>',
                    'data': '0.013 {NAD+}',
                    'refs': [16, 17],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.013},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.015 {4-hydroxy-retinol}',
                    'refs': [107],
                    'substrate': '4-hydroxy-retinol',
                    'units': 'mM',
                    'value': 0.015},
                   {'comment': '#8# recombinant allozyme Val308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.016 {Octanol}',
                    'refs': [115],
                    'substrate': 'Octanol',
                    'units': 'mM',
                    'value': 0.016},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.017 {4-oxo-retinal}',
                    'refs': [107],
                    'substrate': '4-oxo-retinal',
                    'units': 'mM',
                    'value': 0.017},
                   {'chebi': 'CHEBI:16302',
                    'comment': '#8# isozyme ADH1B2, pH 7.5, 25°C <119>',
                    'data': '0.018 {11-cis-retinol}',
                    'refs': [119],
                    'substrate': '11-cis-retinol',
                    'units': 'mM',
                    'value': 0.018},
                   {'data': '0.022 {NAD+}',
                    'refs': [12],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.022},
                   {'chebi': 'CHEBI:78272',
                    'comment': '#8# isozyme ADH1B2, pH 7.5, 25°C <119>',
                    'data': '0.023 {9-cis-retinol}',
                    'refs': [119],
                    'substrate': '9-cis-retinol',
                    'units': 'mM',
                    'value': 0.023},
                   {'chebi': 'CHEBI:17336',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.023 {all-trans-retinol}',
                    'refs': [107],
                    'substrate': 'all-trans-retinol',
                    'units': 'mM',
                    'value': 0.023},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.024 {3,4-dihydro-retinol}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinol',
                    'units': 'mM',
                    'value': 0.024},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.025 {3,4-dihydro-retinal}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinal',
                    'units': 'mM',
                    'value': 0.025},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.025 {4-oxo-retinal}',
                    'refs': [107],
                    'substrate': '4-oxo-retinal',
                    'units': 'mM',
                    'value': 0.025},
                   {'data': '0.025 {NAD+}',
                    'refs': [16],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.025},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.026 {3,4-dihydro-retinal}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinal',
                    'units': 'mM',
                    'value': 0.026},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.027 {4-oxo-retinal}',
                    'refs': [107],
                    'substrate': '4-oxo-retinal',
                    'units': 'mM',
                    'value': 0.027},
                   {'comment': '#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>',
                    'data': '0.027 {5beta-Pregnan-3beta-ol-20-one}',
                    'refs': [116],
                    'substrate': '5beta-Pregnan-3beta-ol-20-one',
                    'units': 'mM',
                    'value': 0.027},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.028 {3,4-dihydro-retinol}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinol',
                    'units': 'mM',
                    'value': 0.028},
                   {'chebi': 'CHEBI:88817',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.032 {3-Phenyl-1-propanol}',
                    'refs': [14],
                    'substrate': '3-Phenyl-1-propanol',
                    'units': 'mM',
                    'value': 0.032},
                   {'chebi': 'CHEBI:17336',
                    'comment': '#8# isozyme ADH1B2, pH 7.5, 25°C <119>; #8# pH '
                               '7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.033 {all-trans-retinol}',
                    'refs': [107, 119],
                    'substrate': 'all-trans-retinol',
                    'units': 'mM',
                    'value': 0.033},
                   {'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.034 {Vanillyl alcohol}',
                    'refs': [14],
                    'substrate': 'Vanillyl alcohol',
                    'units': 'mM',
                    'value': 0.034},
                   {'chebi': 'CHEBI:17898',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.034 {all-trans-retinal}',
                    'refs': [107],
                    'substrate': 'all-trans-retinal',
                    'units': 'mM',
                    'value': 0.034},
                   {'chebi': 'CHEBI:16302',
                    'comment': '#8# isozyme ADH1B1, pH 7.5, 25°C <119>',
                    'data': '0.035 {11-cis-retinol}',
                    'refs': [119],
                    'substrate': '11-cis-retinol',
                    'units': 'mM',
                    'value': 0.035},
                   {'data': '0.044 {Pentanol}',
                    'refs': [96],
                    'substrate': 'Pentanol',
                    'units': 'mM',
                    'value': 0.044},
                   {'comment': '#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>',
                    'data': '0.046 {5beta-androstan-17beta-ol-3-one}',
                    'refs': [116],
                    'substrate': '5beta-androstan-17beta-ol-3-one',
                    'units': 'mM',
                    'value': 0.046},
                   {'data': '0.047 {12-hydroxydodecanoate}',
                    'refs': [96],
                    'substrate': '12-hydroxydodecanoate',
                    'units': 'mM',
                    'value': 0.047},
                   {'data': '0.048 {12-hydroxydodecanoate}',
                    'refs': [53],
                    'substrate': '12-hydroxydodecanoate',
                    'units': 'mM',
                    'value': 0.048},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme beta1,beta1 <17>',
                    'data': '0.049 {ethanol}',
                    'refs': [15, 17],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.049},
                   {'data': '0.056 {12-Hydroxydodecanoic acid}',
                    'refs': [11],
                    'substrate': '12-Hydroxydodecanoic acid',
                    'units': 'mM',
                    'value': 0.056},
                   {'comment': '#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>',
                    'data': '0.058 {5beta-androstan-3beta-ol-17-one}',
                    'refs': [116],
                    'substrate': '5beta-androstan-3beta-ol-17-one',
                    'units': 'mM',
                    'value': 0.058},
                   {'chebi': 'CHEBI:55329',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.06 {16-hydroxyhexadecanoate}',
                    'refs': [14],
                    'substrate': '16-hydroxyhexadecanoate',
                    'units': 'mM',
                    'value': 0.06},
                   {'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '0.08 {Octanol}',
                    'refs': [13],
                    'substrate': 'Octanol',
                    'units': 'mM',
                    'value': 0.08},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#8# isoenzyme beta1,beta1 <15>; #8# isoenzyme '
                               'beta1,beta1, 0.1 M sodium phosphate buffer, pH '
                               '7.5, at 25 °C <20>',
                    'data': '0.085 {acetaldehyde}',
                    'refs': [15, 20],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 0.085},
                   {'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.09 {Pentanol}',
                    'refs': [14],
                    'substrate': 'Pentanol',
                    'units': 'mM',
                    'value': 0.09},
                   {'data': '0.13 {Hexanol}',
                    'refs': [53],
                    'substrate': 'Hexanol',
                    'units': 'mM',
                    'value': 0.13},
                   {'chebi': 'CHEBI:17987',
                    'data': '0.15 {benzyl alcohol}',
                    'refs': [96],
                    'substrate': 'benzyl alcohol',
                    'units': 'mM',
                    'value': 0.15},
                   {'chebi': 'CHEBI:17890',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.2 {tryptophol}',
                    'refs': [14],
                    'substrate': 'tryptophol',
                    'units': 'mM',
                    'value': 0.2},
                   {'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '0.23 {12-hydroxydodecanoate}',
                    'refs': [14],
                    'substrate': '12-hydroxydodecanoate',
                    'units': 'mM',
                    'value': 0.23},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#8# isoenzyme gamma2,gamma2 <15>; #8# isoenzymes '
                               'beta2,beta2 <15>; #8# isoenzyme beta2,beta2, 0.1 M '
                               'sodium phosphate buffer, pH 7.5, 25°C <20>',
                    'data': '0.24 {acetaldehyde}',
                    'refs': [15, 20],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 0.24},
                   {'data': '0.24 {butanol}',
                    'refs': [96],
                    'substrate': 'butanol',
                    'units': 'mM',
                    'value': 0.24},
                   {'comment': '#8# pH 7.3, 37°C, ADH1C*2 (gamma2gamma2) <116>',
                    'data': '0.25 {5beta-cholanic acid-3-one}',
                    'refs': [116],
                    'substrate': '5beta-cholanic acid-3-one',
                    'units': 'mM',
                    'value': 0.25},
                   {'data': '0.28 {Pentanol}',
                    'refs': [53],
                    'substrate': 'Pentanol',
                    'units': 'mM',
                    'value': 0.28},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#8# isoenzyme gamma1,gamma1 <15>',
                    'data': '0.33 {acetaldehyde}',
                    'refs': [15],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 0.33},
                   {'data': '0.34 {NAD+}',
                    'refs': [96],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.34},
                   {'data': '0.55 {1-Octanol}',
                    'refs': [11],
                    'substrate': '1-Octanol',
                    'units': 'mM',
                    'value': 0.55},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme gamma2,gamma2 <15>',
                    'data': '0.63 {ethanol}',
                    'refs': [15],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.63},
                   {'data': '0.79 {butanol}',
                    'refs': [53],
                    'substrate': 'butanol',
                    'units': 'mM',
                    'value': 0.79},
                   {'data': '0.8 {Octanol}',
                    'refs': [21],
                    'substrate': 'Octanol',
                    'units': 'mM',
                    'value': 0.8},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme beta2,beta2, 0.1 M sodium phosphate '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '0.84 {ethanol}',
                    'refs': [20],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.84},
                   {'data': '0.91 {Propanol}',
                    'refs': [96],
                    'substrate': 'Propanol',
                    'units': 'mM',
                    'value': 0.91},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme beta2,beta2 <15>',
                    'data': '0.94 {ethanol}',
                    'refs': [15],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.94},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme gamma1,gamma1 <15>',
                    'data': '1 {ethanol}',
                    'refs': [15],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1.0},
                   {'data': '1.2 {Octanol}',
                    'refs': [16],
                    'substrate': 'Octanol',
                    'units': 'mM',
                    'value': 1.2},
                   {'data': '1.39 {Propanol}',
                    'refs': [53],
                    'substrate': 'Propanol',
                    'units': 'mM',
                    'value': 1.39},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme beta1,beta1 <17>',
                    'data': '1.6 {ethanol}',
                    'refs': [17],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1.6},
                   {'chebi': 'CHEBI:16236',
                    'data': '1.8 {ethanol}',
                    'refs': [10],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1.8},
                   {'chebi': 'CHEBI:17790',
                    'data': '10.4 {methanol}',
                    'refs': [12],
                    'substrate': 'methanol',
                    'units': 'mM',
                    'value': 10.4},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme beta2,beta2, 0.1 M sodium phosphate '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '105 {NADH}',
                    'refs': [20],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 105.0},
                   {'data': '11 {Vanillyl alcohol}',
                    'refs': [16],
                    'substrate': 'Vanillyl alcohol',
                    'units': 'mM',
                    'value': 11.0},
                   {'data': '120 {(S)-2-butanol}',
                    'refs': [53],
                    'substrate': '(S)-2-butanol',
                    'units': 'mM',
                    'value': 120.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '120 {ethanol}',
                    'refs': [14],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 120.0},
                   {'chebi': 'CHEBI:17790',
                    'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '150 {methanol}',
                    'refs': [13],
                    'substrate': 'methanol',
                    'units': 'mM',
                    'value': 150.0},
                   {'data': '17 {Hexanol}',
                    'refs': [21],
                    'substrate': 'Hexanol',
                    'units': 'mM',
                    'value': 17.0},
                   {'chebi': 'CHEBI:16236',
                    'data': '18 {ethanol}',
                    'refs': [96],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 18.0},
                   {'comment': '#8# isoenzyme beta2,beta2, 0.1 M sodium phosphate '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '180 {NAD+}',
                    'refs': [20],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 180.0},
                   {'chebi': 'CHEBI:17935',
                    'data': '2.4 {octanal}',
                    'refs': [16],
                    'substrate': 'octanal',
                    'units': 'mM',
                    'value': 2.4},
                   {'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '210 {Cyclohexanol}',
                    'refs': [14],
                    'substrate': 'Cyclohexanol',
                    'units': 'mM',
                    'value': 210.0},
                   {'comment': '#8# isoenzyme beta1,beta1 <13>',
                    'data': '23 {Cyclohexanol}',
                    'refs': [13],
                    'substrate': 'Cyclohexanol',
                    'units': 'mM',
                    'value': 23.0},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '260 {NADH}',
                    'refs': [20],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 260.0},
                   {'data': '27 {1-Pentanol}',
                    'refs': [11],
                    'substrate': '1-Pentanol',
                    'units': 'mM',
                    'value': 27.0},
                   {'chebi': 'CHEBI:30742',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '290 {ethylene glycol}',
                    'refs': [14],
                    'substrate': 'ethylene glycol',
                    'units': 'mM',
                    'value': 290.0},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '3.4 {acetaldehyde}',
                    'refs': [20],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 3.4},
                   {'chebi': 'CHEBI:28816',
                    'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '310 {2-deoxy-D-ribose}',
                    'refs': [14],
                    'substrate': '2-deoxy-D-ribose',
                    'units': 'mM',
                    'value': 310.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '36 {ethanol}',
                    'refs': [20],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 36.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme alpha,alpha <15,17>',
                    'data': '4.2 {ethanol}',
                    'refs': [15, 17],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 4.2},
                   {'chebi': 'CHEBI:15343',
                    'comment': '#8# isoenzyme alpha,alpha <15>',
                    'data': '4.3 {acetaldehyde}',
                    'refs': [15],
                    'substrate': 'acetaldehyde',
                    'units': 'mM',
                    'value': 4.3},
                   {'chebi': 'CHEBI:30742',
                    'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '50 {ethylene glycol}',
                    'refs': [13],
                    'substrate': 'ethylene glycol',
                    'units': 'mM',
                    'value': 50.0},
                   {'comment': '#8# 0.1 M glycine-NaOH buffer, pH 10.0, 25°C <14>',
                    'data': '560 {2-propanol}',
                    'refs': [14],
                    'substrate': '2-propanol',
                    'units': 'mM',
                    'value': 560.0},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme beta1,beta1, 0.1 M sodium phosphate '
                               'buffer, pH 7.5, at 25 °C <20>',
                    'data': '6.4 {NADH}',
                    'refs': [20],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 6.4},
                   {'comment': '#8# isoenzyme beta1,beta1, 0.1 M sodium phosphate '
                               'buffer, pH 7.5, at 25 °C <20>',
                    'data': '7.4 {NAD+}',
                    'refs': [20],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 7.4},
                   {'comment': '#8# isoenzyme beta3,beta3, 0.1 M sodium phospahte '
                               'buffer, pH 7.5, 25°C <20>',
                    'data': '710 {NAD+}',
                    'refs': [20],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 710.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>',
                    'data': '9 {ethanol}',
                    'refs': [115],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 9.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#12# pH 10.8 <45>; #128# pH 9.0, 22°C, recombinant '
                               'enzyme <222>',
                    'data': '0.45 {ethanol}',
                    'refs': [12, 45, 222],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.45},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme alpha,alpha <17>; #120# mutant '
                               'C257L, pH 8.0, 60°C <246>',
                    'data': '1.5 {ethanol}',
                    'refs': [17, 246],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1.5},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme gamma1,gamma1 <17>; #122# at pH 7.0 '
                               'and 25°C <211>',
                    'data': '3.2 {ethanol}',
                    'refs': [17, 211],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 3.2},
                   {'comment': '#8# isoenzyme beta1,beta1 <16>; #125# 65°C, pH '
                               '10.5 <218>',
                    'data': '0.18 {NAD+}',
                    'refs': [16, 218],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.18},
                   {'chebi': 'CHEBI:16908',
                    'comment': '#8# isoenzyme beta2,beta2 <16>; #150# cosubstrate '
                               'acetoin, pH 6.0, 70°C <243>',
                    'data': '0.105 {NADH}',
                    'refs': [16, 243],
                    'substrate': 'NADH',
                    'units': 'mM',
                    'value': 0.105},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#16# isoenzyme III <79>; #8# isoenzyme '
                               'alpha,gamma1 <13>; #8# isoenzyme gamma2,gamma2 '
                               '<17>',
                    'data': '1.7 {ethanol}',
                    'refs': [13, 17, 79],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 1.7},
                   {'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>; #23# 45°C, pH 8.8, cosubstrate: '
                               '2,3-butanediol, wild-type enzyme <290>',
                    'data': '0.063 {NAD+}',
                    'refs': [115, 290],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.063},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#31# 70°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl <181>; '
                               '#8# isoenzyme beta1,beta1, 0.1 M sodium phosphate '
                               'buffer, pH 7.5, at 25 °C <20>',
                    'data': '0.022 {ethanol}',
                    'refs': [20, 181],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 0.022},
                   {'chebi': 'CHEBI:17336',
                    'comment': '#36# isoenzyme BB-ADH <95>; #8# isozyme ADH1B1, pH '
                               '7.5, 25°C <119>; #8# pH 7.5, 25°C, isozyme ADH1B1 '
                               '<107>',
                    'data': '0.03 {all-trans-retinol}',
                    'refs': [95, 107, 119],
                    'substrate': 'all-trans-retinol',
                    'units': 'mM',
                    'value': 0.03},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#36# isoenzyme TT-ADH <95>',
                    'data': '28 {ethanol}',
                    'refs': [53, 95],
                    'substrate': 'ethanol',
                    'units': 'mM',
                    'value': 28.0},
                   {'comment': '#55# oxidation of ethanol <99>; #8# recombinant '
                               'allozyme Val308, pH 7.5, 25°C <115>',
                    'data': '0.074 {NAD+}',
                    'refs': [99, 115],
                    'substrate': 'NAD+',
                    'units': 'mM',
                    'value': 0.074},
                   {'comment': '#9# isoenzyme ADH-1, pH 10.0 <49>',
                    'data': '0.1 {12-hydroxydodecanoate}',
                    'refs': [16, 49],
                    'substrate': '12-hydroxydodecanoate',
                    'units': 'mM',
                    'value': 0.1}]),
                 ('LO',
                  [{'comment': '#61# 2 isozymes <113>; #24# enzyme polymer forms '
                               'rod-like helical particles <128>',
                    'data': 'cytosol',
                    'refs': [113, 128, 135, 194, 214]}]),
                 ('ME',
                  [{'comment': '#10# activates <87>; #111# dependent on <210>; '
                               '#46# zinc-containing metalloenzyme <164>; '
                               '#88,117,119# catalytic zinc ion <110,111,127>; '
                               '#106# zinc-containing enzyme <161>; #5# 1 '
                               'catalytic and 1 structural zinc ion per subunit '
                               '<119>; #27# 1 catalytic and 1 structural zinc ion '
                               'per subunit, coordination complex geometry <129>; '
                               '#120# 1 catalytic zinc ion and 1 structural zinc '
                               'ion per enzyme subunit <112>; #44# 1 tightly bound '
                               'ion per subunit <114>; #61# ADH I contains 1 Zn2+ '
                               'per subunit, while ADH II does not contains any '
                               'metal ions <113>; #10# all isozymes, amino acid '
                               'residues involved in zinc in binding are Cys46, '
                               'Cys174, His67, Glu68, Asp49, and Thr48, binding '
                               'mode <120>; #8# catalytic zinc <109>; #10# '
                               'included into the crystal strcuture <104>; #10# '
                               'native enzyme contains catalytic zinc ions <122>; '
                               '#106# the catalytic active site zinc ion is bound '
                               'to Glu69 in the apoenzyme state, but not in the '
                               'ternary complex state <108>; #95# ADH is a '
                               'putative zinc-dependent alcohol dehydrogenase '
                               '<162>; #46# contains a zinc ion which is directly '
                               'involved in the structural stabilization of enzyme '
                               'molecule <155>; #46# contains eight zinc atoms per '
                               'tetramer <163>; #6# 1 mM ZnSO4, 1.14fold '
                               'activation <169>; #26# 1 mM ZnSO4, 1.3fold '
                               'activation <188>; #5# 2 atoms are included in each '
                               '40 kDa subunit, while one of the zinc ions is '
                               'considered to serve a structural function only, '
                               'the other zinc ion functions as a Lewis acid and '
                               'activates the substrate in the active site, which '
                               'is located in a cleft between the catalytic and '
                               'the coenzyme binding domain <200>; #122# 20% of '
                               'activity is obtained when replacing Mg2+ with 5 mM '
                               'ZnSO4 <211>; #118# contains Zn2+ <209>; #112# '
                               'maximum activity is reached at 0.5 mM Zn2+,Ta1316 '
                               'ADH is able to tolerate high concentrations of '
                               'Zn2+ <213>; #41# zinc metalloenzyme with two zinc '
                               'atoms per subunit <201>; #123# the enzyme likely '
                               'contains 2 Zn2+ <217>; #6# 1 mM, 114% of initial '
                               'activity <169>; #73# stimulation. Crystal '
                               'structure of alcohol dehydrogenase domain contains '
                               '0.43 Zn atoms per protein monomer <241>; #10# 0.5 '
                               'mM, substrate glycolaldehyde, 32.9% residual '
                               'activity <285>; #161# Pcal_1311 is contains two '
                               'zinc atoms per subunit. Twofold increase in enzyme '
                               'activity of Pcal_1311 when produced in the '
                               'presence of 25 microM Zn2+ as compared to the '
                               'protein produced in tap water <286>',
                    'data': 'Zn2+',
                    'refs': [87,
                             104,
                             108,
                             109,
                             110,
                             111,
                             112,
                             113,
                             114,
                             119,
                             120,
                             122,
                             127,
                             129,
                             155,
                             161,
                             162,
                             163,
                             164,
                             169,
                             188,
                             200,
                             201,
                             209,
                             210,
                             211,
                             213,
                             217,
                             241,
                             285,
                             286]},
                   {'comment': '#106# zinc enzyme <220>; #18# required for '
                               'activity, tightly bound within the enzyme <75>; '
                               '#5# isoenzyme A2 contains 2.7 mol of zinc per mol '
                               'of enzyme, isoenzyme b2 contains 1.9 mol of zinc '
                               'per mol of enzyme, isoenzyme C2 contains 3.2 mol '
                               'of zinc per mol of enzyme. A and C subunits each '
                               'contain two atoms of zinc, with at least one being '
                               'involved catalytically, the b subunit probably '
                               'contains a single non-catalytic zinc atom <48>; '
                               '#9# ADH-1 contains 3.9 mol of zinc per mol of '
                               'subunit, ADH-2 contains 4.2 mol of zinc per mol of '
                               'subunit <49>; #8# enzyme contains 7.59 zinc atoms '
                               'per molecule <96>; #80# contains 3.9 gatom of zinc '
                               'per mol of enzyme <24>; #46# 2 mM required for '
                               'optimal activity <66>; #41# substitution of '
                               'catalytic and /or noncatalytic zinc ions by '
                               'cobaltous ions <36>; #41# contains 4 zinc atoms '
                               'per molecule <42>; #8,12# contains 3.8 mol of Zn '
                               'per mol of protein <16,45>; #42# enzyme form ADH I '
                               'and ADH II contain one zinc atom per subunit <67>; '
                               '#14# contains 1 zinc atom per subunit <81>; #36# '
                               'isoenzyme AA-ADH contains 4.3 zinc atoms per '
                               'dimeric molecule, isoenzyme BB-ADH contains 3.7 '
                               'zinc atoms per dimeric molecule, isoenzyme AA-ADH '
                               'contains 4.1 zinc atoms per dimeric molecule <95>; '
                               '#55# contains 1.2 Zn atom per subunit <99>; #68# '
                               'contains 4 zinc atoms per dimer <69>; #8# zinc '
                               'containing enzyme <12>; #8# from beta1gamma1 and '
                               'gamma1gamma1 isoenzyme the active-site zinc is '
                               'extracted much more slowly than from beta1beta1 '
                               'isoenzyme. Characterization of '
                               'active-site-specific zinc-depleted and '
                               'reconstituted cobalt(II) alcohol dehydrogenase '
                               '<19>; #8# contains 3.7 gatom of zinc per mol of '
                               'enzyme <23>; #8# 3.6-4.2 gatom of zinc per mol '
                               '<21>; #43# contains 3.7-4.2 mol of zinc per mol of '
                               'enzyme <25>; #104# KmADH3 appears to belong to the '
                               'zinc-containing Adh family <177>; #105# KmADH4 '
                               'appears to belong to the zinc-containing Adh '
                               'family <177>',
                    'data': 'Zinc',
                    'refs': [12,
                             16,
                             19,
                             21,
                             23,
                             24,
                             25,
                             36,
                             42,
                             45,
                             48,
                             49,
                             66,
                             67,
                             69,
                             70,
                             75,
                             81,
                             95,
                             96,
                             99,
                             177,
                             220]}]),
                 ('MW',
                  [{'comment': '#113# SDS-PAGE <197>; #107# isozyme ADH2, apparent '
                               'molecular weight deduced from electrophoretic '
                               'mobility <214>; #110# isozyme ADH4, calculated '
                               'from amino acid sequence <214>; #93,133# 4 * '
                               '40000, SDS-PAGE <144,239>; #8,10,36,53,80# 2 * '
                               '40000, SDS-PAGE <16,23,24,59,87,95>; #1,8,81,132# '
                               'x * 40000, SDS-PAGE <11,44,52,227>; #9# 2 * 40000, '
                               'ADH-3, SDS-PAGE <49>; #42# 2 * 40000, enzyme form '
                               'ADHI <68>',
                    'data': '40000',
                    'refs': [11,
                             16,
                             23,
                             24,
                             44,
                             49,
                             52,
                             59,
                             68,
                             87,
                             95,
                             144,
                             197,
                             214,
                             227,
                             239,
                             272]},
                   {'comment': '#8# ultracentrifugation under non-denaturing '
                               'conditions <23>',
                    'data': '78000',
                    'refs': [23]},
                   {'comment': '#8# amino acid analysis, ultracentrifugation <18>',
                    'data': '78000-85000',
                    'refs': [18]},
                   {'comment': '#8# ultracentrifugal analysis <21>',
                    'data': '79000-84000',
                    'refs': [21]},
                   {'comment': '#8# equilibrium sedimentation <16>',
                    'data': '82700',
                    'refs': [16]},
                   {'comment': '#70# 4 * 42000, SDS-PAGE <84>; #8# x * 42000, '
                               'SDS-PAGE <14>; #68# 2 * 42000, SDS-PAGE <69>; #8# '
                               '2 * 42000, anodic enzyme form, SDS-PAGE <18>; #69# '
                               '2 * 42000, enzyme form ADH-2 and ADH-3, SDS-PAGE '
                               '<60>; #61# 3 * 42000, ADH I, SDS-PAGE <113>; #23# '
                               'fusion protein, bet-AshD <289>',
                    'data': '42000',
                    'refs': [14, 18, 60, 69, 84, 113, 289]},
                   {'comment': '#36# 2 * 41000, SDS-PAGE <47>; #8# 2 * 41000, '
                               'class III isoenzyme chi ADH, SDS-PAGE <16>',
                    'data': '41000',
                    'refs': [16, 47]}]),
                 ('NSP',
                  [{'comment': '#8# ADH4 might be involved in biosynthesis of '
                               'retinoic acid <124>',
                    'data': 'all-trans-retinol + NAD+ = all-trans-retinal + NADH',
                    'refs': [124, 200]},
                   {'comment': '#8# ADH4 might be involved in biosynthesis of '
                               'retinoic acid <124>) {r',
                    'data': 'all-trans-retinol + NAD+ = all-trans-retinal + NADH',
                    'refs': [124, 200]},
                   {'comment': '#5# role of the major liver isoenzyme A2 in '
                               'ethanol metabolism <48>; #41# plays an important '
                               'role in the metabolism of ethanol <102>; #8# '
                               'chi-ADH plays an important role in the metabolism '
                               'of long chain alcohols and aldehydes <21>; #8# the '
                               'anodic enzyme form may contribute significantly to '
                               'alcohol elimination in man, particularly at high '
                               'concentrations when the other enzyme species are '
                               'saturated <18>; #8# the enzyme plays a significant '
                               'role in first-pass metabolism of ethanol in human '
                               '<96>; #8# enzyme is responsible for the major '
                               'ethanol oxidation capacity in the body. The '
                               'products acetaldehyde and NADH are responsible for '
                               'the most of the toxic effects and metabolic '
                               'disturbances produced by ethanol ingestion <10>; '
                               '#10# rate-limiting step of the alcoholic '
                               'fermentation <122>; #5# DH3 plays an important '
                               'role in systemic ethanol metabolism at higher '
                               'levels of blood ethanol through activation by '
                               'cytoplasmic solution hydrophobicity <141>',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH',
                    'refs': [10, 18, 21, 48, 96, 102, 116, 122, 141, 181]},
                   {'comment': '#5# role of the major liver isoenzyme A2 in '
                               'ethanol metabolism <48>; #41# plays an important '
                               'role in the metabolism of ethanol <102>; #8# '
                               'chi-ADH plays an important role in the metabolism '
                               'of long chain alcohols and aldehydes <21>; #8# the '
                               'anodic enzyme form may contribute significantly to '
                               'alcohol elimination in man, particularly at high '
                               'concentrations when the other enzyme species are '
                               'saturated <18>; #8# the enzyme plays a significant '
                               'role in first-pass metabolism of ethanol in human '
                               '<96>; #8# enzyme is responsible for the major '
                               'ethanol oxidation capacity in the body. The '
                               'products acetaldehyde and NADH are responsible for '
                               'the most of the toxic effects and metabolic '
                               'disturbances produced by ethanol ingestion <10>; '
                               '#10# rate-limiting step of the alcoholic '
                               'fermentation <122>; #5# DH3 plays an important '
                               'role in systemic ethanol metabolism at higher '
                               'levels of blood ethanol through activation by '
                               'cytoplasmic solution hydrophobicity <141>) {r',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH',
                    'refs': [10, 18, 21, 48, 96, 102, 116, 122, 141, 181]},
                   {'data': '1-butanol + NAD+ = butanal + NADH + H+',
                    'refs': [229]},
                   {'data': '1-butanol + NAD+ = butanal + NADH + H+ {r}',
                    'refs': [229]},
                   {'data': 'isobutyramide + NAD+ = ? {r}', 'refs': [124]},
                   {'comment': '#10# constitutive enzyme <94>; #42# key enzyme in '
                               'ethanol production <68>; #52# one constitutive '
                               'enzyme, ADH-MI and one inducible enzyme, ADH-MII '
                               '<82>; #53# enzyme may be involved in the '
                               'metabolism of dietary wax esters in salmonid fish '
                               '<59>; #79# the enzyme oxidizes alcohols to '
                               'aldehydes or ketones both for detoxification and '
                               'metabolic purposes <38>; #36# involvement in the '
                               'development of male hamster reproductive system '
                               '<47>; #60# alcohol dehydrogenase activity may not '
                               'limit alcohol supply for ester production during '
                               'ripening <146>; #41# activity is severely reduced '
                               'towards aliphatic alcohols of more than 8 carbon '
                               'atoms for the free enzyme, but not so with '
                               'immobilized HLAD, exhibiting an activity towards '
                               'C22 and C24 aliphatic alcohols higher than 50% of '
                               'the highest value, obtained with C8 <204>; #8# '
                               'differences in the activities of total ADH and '
                               'class I ADH isoenzyme between cancer liver tissues '
                               'and healthy hepatocytes may be a factor in ethanol '
                               'metabolism disorders, which can intensify '
                               'carcinogenesis <180>; #113# TADH is a '
                               'NAD(H)-dependent enzyme and shows a very broad '
                               'substrate spectrum producing exclusively the '
                               '(S)-enantiomer in high enantiomeric excess (more '
                               'than 99%) during asymmetric reduction of ketones '
                               '<197>; #124# the physiological direction of the '
                               'catalytic reaction is reduction rather than '
                               'oxidation <219>',
                    'data': 'more = ?',
                    'refs': [38, 47, 59, 68, 82, 94, 146, 180, 197, 204, 219]}]),
                 ('PHO',
                  [{'comment': '#5,8# assay at <107,124,200>; #55# reduction of '
                               'acetaldehyde <99>; #3# reduction of substrate <4>; '
                               '#76# and second optimum at pH 9.9 <64>; #46# '
                               'reduction of anisaldehyde <66>; #8# kinetic '
                               'analysis assay at <115>; #10# Zn-ADH, Co-ADH, and '
                               'Cu-ADH <122>; #10# enzyme covalently immobilized '
                               'to magnetic Fe3O4 nanoparticles via glutaraldehyde '
                               '<182>; #10# immobilized enzyme, at 25°C <196>; #8# '
                               'assay at, class IV enzyme, reduction reaction '
                               '<229>',
                    'data': '7.5',
                    'refs': [4,
                             64,
                             66,
                             99,
                             107,
                             115,
                             122,
                             124,
                             182,
                             196,
                             200,
                             229]},
                   {'comment': '#3# oxidation of substrate <4>; #18# wild-type '
                               'enzyme ADH1-1S <97>; #46# oxidation of benzyl '
                               'alcohol <66>; #8# isoenzyme beta2,beta2 <20>; '
                               '#129# oxidation reaction <225>; #61# assay at, '
                               'forward reaction, ADH I and ADH II <113>; #8# '
                               'isozyme ADH1B2, assay at <119>; #46# mutant enzyme '
                               'N249Y <154>; #8# assay at, total ADH activity '
                               '<229>',
                    'data': '8.5',
                    'refs': [4, 20, 66, 97, 105, 113, 119, 154, 225, 229]},
                   {'comment': '#119# assay at <111>; #120# oxidation of ethanol '
                               '<256>; #4,72# and a second optimum at pH 9.5 <64>; '
                               '#18# mutant enzyme ADH1-1S1108 <97>; #48# aldehyde '
                               'reduction <223>; #8# assay at, class III enzyme, '
                               'reduction reaction <229>; #133# reduction of '
                               '2-pentanone <239>; #151# oxidation of crotyl '
                               'aclohol <244>',
                    'data': '8',
                    'refs': [64, 97, 106, 111, 215, 223, 229, 239, 244, 252, 256]},
                   {'comment': '#5# assay at <119>; #74# oxidation of ethanol <2>; '
                               '#8# isoenzyme beta1,beta1 <20>; #8# isozyme '
                               'ADH1B1, ADH4, assay at <119>; #123# oxidation of '
                               '1-hexanol <217>; #133# oxidation of 2-pentanol '
                               '<239>',
                    'data': '10.5',
                    'refs': [2, 10, 20, 119, 217, 239, 284]},
                   {'comment': '#8# and a second optimum at pH 10.0-10.5, ADH '
                               'Indianapolis form 2 and 3 <22>',
                    'data': '10-10.5',
                    'refs': [22]},
                   {'comment': '#8# acetaldehyde reduction of isoenzyme '
                               'beta2,beta2 <15>',
                    'data': '7.4',
                    'refs': [15]},
                   {'comment': '#8# assay at, class II enzyme, reduction reaction '
                               '<229>',
                    'data': '7.6',
                    'refs': [229]},
                   {'comment': '#8# ethanol oxidation, isoenzyme beta2,beta2, '
                               'beta2,beta1, alpha,beta2 and beta2gamma1 <15>',
                    'data': '8.5-8.8',
                    'refs': [15]},
                   {'comment': '#163# assay at <288>; #164# assay <291>; #8# '
                               'isoenzyme beta3,beta3 <20>; #8# ADH Indianapolis '
                               'form 1 <22>; #123# reduction of benzaldehyde '
                               '<217>; #10# free enzyme, at 25°C <196>',
                    'data': '7',
                    'refs': [20, 22, 82, 132, 196, 217, 252, 288, 291]},
                   {'comment': '#12# and a second lower maximum at pH 7.5 <45>',
                    'data': '10.8',
                    'refs': [12, 45]},
                   {'comment': '#8# and a second optimum at pH 10.0-10.5, ADH '
                               'Indianapolis form 2 and 3 <22>; #122# for ethanol '
                               'oxidation <211>',
                    'data': '7-7.5',
                    'refs': [22, 211]},
                   {'comment': '#130# assay at <230>; #42# enzyme form ADH-II, '
                               'oxidation of ethanol <67,68>; #8# standard assay '
                               'at <115>; #125# alcohol oxidation reaction <218>; '
                               '#134# optimally active with 1-butanol at pH 10.0 '
                               'with 4 M KCl <237>; #161# glycine\x96NaOH buffer, '
                               'highest activity for oxidation of ethanol <286>',
                    'data': '10',
                    'refs': [67, 68, 75, 96, 115, 118, 218, 230, 237, 286]},
                   {'comment': '#8# acetaldehyde reduction, isoenzyme beta1,beta1 '
                               '<15>',
                    'data': '5.9',
                    'refs': [15, 133]},
                   {'comment': '#8,41# assay at <116,117>',
                    'data': '7.3',
                    'refs': [116, 117]},
                   {'comment': '#47# oxidation of 2-phenylethanol <149>',
                    'data': '10.4',
                    'refs': [14, 149]}]),
                 ('PHR',
                  [{'comment': '#8# pH 8.0: about 40% of maximal activity, pH '
                               '10.5: about 85% of maximal activity <96>',
                    'data': '8-10.5',
                    'refs': [96]},
                   {'comment': '#8# about 30% of maximal activity at pH 8.0 and at '
                               'pH 12.0 <14>; #47# pH 8.0: about 50% of maximal '
                               'activity, pH 12.0: about 50% of maximal activity, '
                               'oxidation of 2-phenylethanol <149>; #31# pH 8.0: '
                               'about 70% of maximal activity, pH 12: about 60% of '
                               'maximal activity <181>',
                    'data': '8-12',
                    'refs': [14, 149, 181]}]),
                 ('PHS',
                  [{'comment': '#8# stable <12>', 'data': '7-10.6', 'refs': [12]}]),
                 ('PU',
                  [{'data': '(anodic enzyme form)', 'refs': [18]},
                   {'data': '(class I isoenzymes)', 'refs': [13]},
                   {'data': '(class II isoenzyme: pi-ADH)', 'refs': [14]},
                   {'data': '(class III isoenzyme chi-ADH)', 'refs': [16]},
                   {'data': '(isoenzyme beta3,beta3)', 'refs': [20]},
                   {'data': '(recombinant ADH2 alloenzymes from Escherichia coli '
                            'by DEAE and AMP or blue Sepharose chromatography, and '
                            'ultrafiltration)',
                    'refs': [115]},
                   {'data': '(recombinant enzyme from Escherichia coli by DEAE ion '
                            "exchange, 5'-AMP-resin affinity, and Mono Q ion "
                            'exchange chromatography)',
                    'refs': [124]},
                   {'data': '(recombinant isozymes from Escherichia coli strain '
                            'BL21)',
                    'refs': [119]},
                   {'data': '', 'refs': [12, 15]}]),
                 ('RE',
                  {'a primary alcohol + NAD+ = an aldehyde + NADH + H+ (#4,41# '
                   'ordered bi-bi mechanism <31,43>; #4,76# rapid equilibrium '
                   'random mechanism <63>; #8# ordered bi bi mechanism with '
                   'cofactor adding first to form a binary enzyme complex <23>; '
                   '#41# isoenzyme EE and SS: ordered bi bi mechanism <35>; '
                   '#10,33# mechanism is predominantly ordered with ethanol, but '
                   'partially random with butanol <91>; #41# kinetic mechanism is '
                   'random for ethanol oxidation and compulsory ordered for '
                   'acetaldehyde reduction <41>; #38# oxidizes ethanol in an '
                   'ordered bi-bi mechanism with NAD+ as the first substrate fixed '
                   '<85>; #10# compulsory-order mechanism with the rate-limiting '
                   'step being the dissociation of the product enzyme-NAD+ complex '
                   '<90>; #28,68,79# Theorell-Chance mechanism <38,69,74>; #44# '
                   'sequential reaction mechanism <114>; #88# active site '
                   'structure <127>; #79# catalytic mechanism involves a proton '
                   'relay modulated by the coupled ionization of the active site '
                   'Lys155/Tyr151 pair, and a NAD+ ribose 2-OH switch, other '
                   'active site residues are Ser138 and Trp144, ionization '
                   'properties, substrate binding, overview <130>; #8# class IV '
                   'alcohol dehydrogenase also functions as retinol dehydrogenase, '
                   'reaction and kinetic mechanism: asymmetric rapid equilibrium '
                   'random mechanism with 2 dead-end ternary complexes fro retinol '
                   'oxidation and a rapid equilibrium ordered mechanism with one '
                   'dead-end ternary complex for retinal reduction, a unique '
                   'mechanistic form fro zinc-containing ADH in the medium chain '
                   'dehydrogenase/reductase superfamily of enzymes <124>; #10# '
                   'detailed determination of the reaction and kinetic mechanisms, '
                   'active site structure and determination of amino acid residues '
                   'involved in catalysis, 3 isozymes <120>; #117# ordered bibi '
                   'mechanism, structural and functional implications of amino '
                   'acid residue 47 <110>; #41# ordered sequential bibi reaction '
                   'mechanism, modeling of oxidation kinetic mechanism <117>; '
                   '#119# reaction mechanism, His51 is involved, but not '
                   'essential, in catalysis facilitating the deprotonation of the '
                   'hydroxyl group of water or alcohol ligated to the catalytic '
                   'zinc <111>; #8# Ser48 is involved in catalysis, isozyme '
                   'gamma(2)gamma(2) <109>; #27# the catalytic triad consists of '
                   'Cys44, His67, and Cys154, active site structure <129>)',
                   'a secondary alcohol + NAD+ = a ketone + NADH + H+'}),
                 ('RN', {'alcohol dehydrogenase'}),
                 ('RT', {'redox reaction', 'reduction', 'oxidation'}),
                 ('SA',
                  [{'data': '0.6',
                    'refs': [16],
                    'units': 'µmol/min/mg',
                    'value': 0.6},
                   {'data': '0.65',
                    'refs': [21],
                    'units': 'µmol/min/mg',
                    'value': 0.65},
                   {'data': '1.47',
                    'refs': [14],
                    'units': 'µmol/min/mg',
                    'value': 1.47},
                   {'data': '3.3',
                    'refs': [12],
                    'units': 'µmol/min/mg',
                    'value': 3.3},
                   {'comment': '#9# ADH-3 <49>',
                    'data': '1.3',
                    'refs': [18, 49],
                    'units': 'µmol/min/mg',
                    'value': 1.3}]),
                 ('SN', {'alcohol:NAD+ oxidoreductase'}),
                 ('SP',
                  [{'comment': '#89# best substrate <118>; #8# class III isoenzyme '
                               'chi-ADH oxidizes ethanol very poorly <16>; #8# no '
                               'oxidation with class III enzyme <11>; #9# '
                               'isoenzyme ADH-1 and ADH-3, no activity with '
                               'isoenzyme ADH-2 <49>; #55# the reduction of '
                               'acetaldehyde is 4.9fold faster than the oxidation '
                               'of ethanol <99>; #52# the reduction of '
                               'acetaldehyde of ADH-MII is about 7times higher '
                               'than that of the oxidation of ethanol <82>; #5# no '
                               'activity with isoenzyme B2, oxidized by isoenzyme '
                               'A2 and C2 <48>; #5# role of the major liver '
                               'isoenzyme A2 in ethanol metabolism <48>; #41# '
                               'plays an important role in the metabolism of '
                               'ethanol <102>; #8# chi-ADH plays an important role '
                               'in the metabolism of long chain alcohols and '
                               'aldehydes <21>; #8# the anodic enzyme form may '
                               'contribute significantly to alcohol elimination in '
                               'man, particularly at high concentrations when the '
                               'other enzyme species are saturated <18>; #8# the '
                               'enzyme plays a significant role in first-pass '
                               'metabolism of ethanol in human <96>; #8# enzyme is '
                               'responsible for the major ethanol oxidation '
                               'capacity in the body. The products acetaldehyde '
                               'and NADH are responsible for the most of the toxic '
                               'effects and metabolic disturbances produced by '
                               'ethanol ingestion <10>; #10# rate-limiting step of '
                               'the alcoholic fermentation <122>; #119# '
                               'isomerization of the enzyme-NAD+ complex is the '
                               'rate-limiting step for acetaldehyde reduction by '
                               'the wild-type enzyme <111>; #91# no cooperativity '
                               'between the 2 active sites of the enzyme <105>; '
                               '#5# DH3 plays an important role in systemic '
                               'ethanol metabolism at higher levels of blood '
                               'ethanol through activation by cytoplasmic solution '
                               'hydrophobicity <141>; #47# 76% of the activity '
                               'with 2-phenylethanol <149>; #120# proton and '
                               'hydride equivalent transfer in the alcohol '
                               'dehydrogenase enzymatic reaction are modulated by '
                               'the correlated motions between NAD+ and the '
                               'cofactor domain <176>) |#61# acetaldehyde is the '
                               'best substrate for isozyme ADH I <113>',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH',
                    'refs': [2,
                             6,
                             10,
                             11,
                             12,
                             13,
                             14,
                             16,
                             17,
                             18,
                             20,
                             21,
                             24,
                             25,
                             28,
                             35,
                             41,
                             42,
                             43,
                             45,
                             47,
                             48,
                             49,
                             51,
                             52,
                             53,
                             59,
                             60,
                             64,
                             65,
                             67,
                             68,
                             69,
                             71,
                             72,
                             73,
                             74,
                             75,
                             76,
                             77,
                             78,
                             81,
                             82,
                             83,
                             84,
                             87,
                             90,
                             92,
                             95,
                             96,
                             97,
                             99,
                             101,
                             102,
                             105,
                             111,
                             113,
                             115,
                             116,
                             117,
                             118,
                             119,
                             120,
                             121,
                             122,
                             126,
                             128,
                             135,
                             141,
                             147,
                             149,
                             170,
                             172,
                             176,
                             181]},
                   {'comment': '#89# best substrate <118>; #8# class III isoenzyme '
                               'chi-ADH oxidizes ethanol very poorly <16>; #8# no '
                               'oxidation with class III enzyme <11>; #9# '
                               'isoenzyme ADH-1 and ADH-3, no activity with '
                               'isoenzyme ADH-2 <49>; #55# the reduction of '
                               'acetaldehyde is 4.9fold faster than the oxidation '
                               'of ethanol <99>; #52# the reduction of '
                               'acetaldehyde of ADH-MII is about 7times higher '
                               'than that of the oxidation of ethanol <82>; #5# no '
                               'activity with isoenzyme B2, oxidized by isoenzyme '
                               'A2 and C2 <48>; #5# role of the major liver '
                               'isoenzyme A2 in ethanol metabolism <48>; #41# '
                               'plays an important role in the metabolism of '
                               'ethanol <102>; #8# chi-ADH plays an important role '
                               'in the metabolism of long chain alcohols and '
                               'aldehydes <21>; #8# the anodic enzyme form may '
                               'contribute significantly to alcohol elimination in '
                               'man, particularly at high concentrations when the '
                               'other enzyme species are saturated <18>; #8# the '
                               'enzyme plays a significant role in first-pass '
                               'metabolism of ethanol in human <96>; #8# enzyme is '
                               'responsible for the major ethanol oxidation '
                               'capacity in the body. The products acetaldehyde '
                               'and NADH are responsible for the most of the toxic '
                               'effects and metabolic disturbances produced by '
                               'ethanol ingestion <10>; #10# rate-limiting step of '
                               'the alcoholic fermentation <122>; #119# '
                               'isomerization of the enzyme-NAD+ complex is the '
                               'rate-limiting step for acetaldehyde reduction by '
                               'the wild-type enzyme <111>; #91# no cooperativity '
                               'between the 2 active sites of the enzyme <105>; '
                               '#5# DH3 plays an important role in systemic '
                               'ethanol metabolism at higher levels of blood '
                               'ethanol through activation by cytoplasmic solution '
                               'hydrophobicity <141>; #47# 76% of the activity '
                               'with 2-phenylethanol <149>; #120# proton and '
                               'hydride equivalent transfer in the alcohol '
                               'dehydrogenase enzymatic reaction are modulated by '
                               'the correlated motions between NAD+ and the '
                               'cofactor domain <176>) |#61# acetaldehyde is the '
                               'best substrate for isozyme ADH I <113>| {r',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH',
                    'refs': [2,
                             6,
                             10,
                             11,
                             12,
                             13,
                             14,
                             16,
                             17,
                             18,
                             20,
                             21,
                             24,
                             25,
                             28,
                             35,
                             41,
                             42,
                             43,
                             45,
                             47,
                             48,
                             49,
                             51,
                             52,
                             53,
                             59,
                             60,
                             64,
                             65,
                             67,
                             68,
                             69,
                             71,
                             72,
                             73,
                             74,
                             75,
                             76,
                             77,
                             78,
                             81,
                             82,
                             83,
                             84,
                             87,
                             90,
                             92,
                             95,
                             96,
                             97,
                             99,
                             101,
                             102,
                             105,
                             111,
                             113,
                             115,
                             116,
                             117,
                             118,
                             119,
                             120,
                             121,
                             122,
                             126,
                             128,
                             135,
                             141,
                             147,
                             149,
                             170,
                             172,
                             176,
                             181]},
                   {'comment': '#10# no activity <87>; #42# very low activity '
                               '<67>; #55# 3% of the activity with ethanol <99>',
                    'data': 'propan-2-ol + NAD+ = acetone + NADH',
                    'refs': [14,
                             43,
                             45,
                             61,
                             64,
                             65,
                             66,
                             67,
                             68,
                             81,
                             84,
                             85,
                             87,
                             90,
                             92,
                             97,
                             99]},
                   {'data': 'propanol + NADH = propionaldehyde + NADH',
                    'refs': [20,
                             45,
                             53,
                             59,
                             61,
                             65,
                             66,
                             67,
                             68,
                             71,
                             75,
                             77,
                             78,
                             83,
                             84,
                             85,
                             87,
                             90,
                             96,
                             97,
                             99]},
                   {'comment': '#18# no activity <97>; #18# weak activity <75>; '
                               '#41# (R)-2-butanol and (S)-2-butanol <31>',
                    'data': 'butan-2-ol + NAD+ = butan-2-one + NADH',
                    'refs': [20,
                             31,
                             47,
                             53,
                             59,
                             61,
                             64,
                             66,
                             75,
                             83,
                             84,
                             85,
                             92,
                             95,
                             97]},
                   {'comment': '#10# weak <87>; #42# activity with ADH I, no '
                               'activity with ADH II <68>; #42# oxidized by enzyme '
                               'form ADH-I, no activity with enzyme form ADH-II '
                               '<67>; #9# pH 10.0: oxidized by ADH-1 and ADH-3, no '
                               'activity with isoenzyme ADH-2 <49>',
                    'data': 'butanol + NAD+ = butyraldehyde + NADH',
                    'refs': [16,
                             18,
                             20,
                             42,
                             45,
                             47,
                             49,
                             53,
                             59,
                             60,
                             61,
                             64,
                             66,
                             67,
                             68,
                             75,
                             77,
                             78,
                             83,
                             85,
                             87,
                             90,
                             95,
                             96,
                             97,
                             101]},
                   {'data': '7-cis-retinol + NAD+ = 7-cis-retinal + NADH',
                    'refs': [119]},
                   {'comment': '#48# best substrate <223>; #79,112# 100% activity '
                               '<61,213>; #101# no activity with NADP+, in reverse '
                               'reaction no activity with NADPH <171>; #31# the '
                               'enzyme is highly specific for ethanol with NAD+ as '
                               'the coenzyme <181>; #113# 88% activity compared to '
                               'cyclohexanol <197>; #107# substrate for isozyme '
                               'ADH1C, extremely poor substrate for isozyme ADH3 '
                               '<214>; #107# substrate for isozyme ADH2 <214>; '
                               '#110# substrate for isozyme ADH4 <214>; #134# the '
                               'enzyme shows a preference for short-chain alcohols '
                               'ethanol and 1-propanol <237>; #155# 12% of the '
                               'activity with butan-1-ol <271>; #161# 33% of the '
                               'activity with 1,4-butanediol <286>) |#120# 83% of '
                               'the activity with butan-2-ol <256>',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH + H+',
                    'refs': [61,
                             66,
                             79,
                             85,
                             103,
                             136,
                             139,
                             140,
                             143,
                             144,
                             147,
                             148,
                             153,
                             159,
                             161,
                             162,
                             163,
                             171,
                             173,
                             174,
                             181,
                             194,
                             195,
                             196,
                             197,
                             203,
                             205,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             222,
                             223,
                             231,
                             233,
                             237,
                             239,
                             246,
                             252,
                             256,
                             271,
                             277,
                             279,
                             284,
                             286,
                             288]},
                   {'comment': '#48# best substrate <223>; #79,112# 100% activity '
                               '<61,213>; #101# no activity with NADP+, in reverse '
                               'reaction no activity with NADPH <171>; #31# the '
                               'enzyme is highly specific for ethanol with NAD+ as '
                               'the coenzyme <181>; #113# 88% activity compared to '
                               'cyclohexanol <197>; #107# substrate for isozyme '
                               'ADH1C, extremely poor substrate for isozyme ADH3 '
                               '<214>; #107# substrate for isozyme ADH2 <214>; '
                               '#110# substrate for isozyme ADH4 <214>; #134# the '
                               'enzyme shows a preference for short-chain alcohols '
                               'ethanol and 1-propanol <237>; #155# 12% of the '
                               'activity with butan-1-ol <271>; #161# 33% of the '
                               'activity with 1,4-butanediol <286>) |#120# 83% of '
                               'the activity with butan-2-ol <256>| {r',
                    'data': 'ethanol + NAD+ = acetaldehyde + NADH + H+',
                    'refs': [61,
                             66,
                             79,
                             85,
                             103,
                             136,
                             139,
                             140,
                             143,
                             144,
                             147,
                             148,
                             153,
                             159,
                             161,
                             162,
                             163,
                             171,
                             173,
                             174,
                             181,
                             194,
                             195,
                             196,
                             197,
                             203,
                             205,
                             207,
                             208,
                             209,
                             210,
                             211,
                             212,
                             213,
                             214,
                             222,
                             223,
                             231,
                             233,
                             237,
                             239,
                             246,
                             252,
                             256,
                             271,
                             277,
                             279,
                             284,
                             286,
                             288]},
                   {'data': 'octanol + NAD+ = octanal + NADH',
                    'refs': [110, 115, 200]},
                   {'comment': '#8# ADH4 might be involved in biosynthesis of '
                               'retinoic acid <124>',
                    'data': 'all-trans-retinol + NAD+ = all-trans-retinal + NADH',
                    'refs': [47, 53, 93, 95, 107, 119, 124, 200]},
                   {'comment': '#8# ADH4 might be involved in biosynthesis of '
                               'retinoic acid <124>) {r',
                    'data': 'all-trans-retinol + NAD+ = all-trans-retinal + NADH',
                    'refs': [47, 53, 93, 95, 107, 119, 124, 200]},
                   {'comment': '#42# activity with ADH I, no activity with ADH II '
                               '<68>',
                    'data': 'hexanol + NAD+ = n-hexanal + NADH',
                    'refs': [20, 21, 42, 48, 53, 68, 84, 92, 95, 101]},
                   {'comment': '#69# no activity <60>; #8# class III isoenzyme '
                               'chi-ADH shows no activity <16>; #5# oxidized by '
                               'isoenzyme A2, no activity with isoenzyme B2 and C2 '
                               '<48>',
                    'data': 'ethylene glycol + NAD+ = ? + NADH',
                    'refs': [13, 14, 16, 48, 60, 85]},
                   {'data': '11-cis-retinol + NAD+ = 11-cis-retinal + NADH',
                    'refs': [93, 119]},
                   {'comment': '#5,8# no activity with isozyme ADH1 <119>',
                    'data': '13-cis-retinol + NAD+ = 13-cis-retinal + NADH',
                    'refs': [93, 119]},
                   {'data': '9-cis-retinol + NAD+ = 9-cis-retinal + NADH',
                    'refs': [93, 119]},
                   {'comment': '#5# oxidized by isoenzyme A2 and B2, no activity '
                               'with isoenzyme C2 <48>',
                    'data': 'pentanal + NAD+ = pentanone + NADH',
                    'refs': [14, 16, 18, 20, 24, 25, 48, 53, 84, 92, 96]},
                   {'comment': '#8,18,38,42,69,70# no activity '
                               '<21,60,67,68,75,84,85>; #89# low activity <118>; '
                               '#52# reaction is extremly weak <82>; #8# anodic '
                               'enzyme form shows no activity <18>; #12# no '
                               'activity at pH 7.5, slight activity at pH 10.8 '
                               '<45>; #5# weak activity with isoenzyme A2, no '
                               'activity with isoenzyme B2 and C2 <48>; #9# '
                               'oxidized with ADH-3, no activity with ADH-1 and '
                               'ADH-2 <49>; #8# class I isoenzymes <13>; #8# no '
                               'activity with isoenzyme beta3,beta3 <20>; #80# '
                               'reaction is catalyzed by the pyrazole-sensitive '
                               'enzyme, no activity with the pyrazole-insensitive '
                               'enzyme <24>; #43# reaction is catalyzed by the '
                               'cathodic pyrazole-sensitive enzyme, no activity by '
                               'the cathodic pyrazole-insensitive enzyme and by '
                               'the anodic pyrazole-insensitive enzyme <25>; #8# '
                               'activity detected with class II isoenzyme pi-ADH '
                               '<14>; #8# oxidized by isoenzyme beta1,beta1 <20>; '
                               '#8# class III isoenzyme chi-ADH shows no activity '
                               '<16>; #8# no activity with class III enzyme <11>; '
                               '#112# 49.9% activity compared to ethanol <213>',
                    'data': 'methanol + NAD+ = formaldehyde + NADH + H+',
                    'refs': [11,
                             12,
                             13,
                             14,
                             16,
                             18,
                             20,
                             21,
                             24,
                             25,
                             45,
                             48,
                             49,
                             59,
                             60,
                             66,
                             67,
                             68,
                             75,
                             82,
                             84,
                             85,
                             101,
                             118,
                             147,
                             171,
                             173,
                             213]},
                   {'comment': '#8,18,38,42,69,70# no activity '
                               '<21,60,67,68,75,84,85>; #89# low activity <118>; '
                               '#52# reaction is extremly weak <82>; #8# anodic '
                               'enzyme form shows no activity <18>; #12# no '
                               'activity at pH 7.5, slight activity at pH 10.8 '
                               '<45>; #5# weak activity with isoenzyme A2, no '
                               'activity with isoenzyme B2 and C2 <48>; #9# '
                               'oxidized with ADH-3, no activity with ADH-1 and '
                               'ADH-2 <49>; #8# class I isoenzymes <13>; #8# no '
                               'activity with isoenzyme beta3,beta3 <20>; #80# '
                               'reaction is catalyzed by the pyrazole-sensitive '
                               'enzyme, no activity with the pyrazole-insensitive '
                               'enzyme <24>; #43# reaction is catalyzed by the '
                               'cathodic pyrazole-sensitive enzyme, no activity by '
                               'the cathodic pyrazole-insensitive enzyme and by '
                               'the anodic pyrazole-insensitive enzyme <25>; #8# '
                               'activity detected with class II isoenzyme pi-ADH '
                               '<14>; #8# oxidized by isoenzyme beta1,beta1 <20>; '
                               '#8# class III isoenzyme chi-ADH shows no activity '
                               '<16>; #8# no activity with class III enzyme <11>; '
                               '#112# 49.9% activity compared to ethanol <213>) '
                               '{ir',
                    'data': 'methanol + NAD+ = formaldehyde + NADH + H+',
                    'refs': [11,
                             12,
                             13,
                             14,
                             16,
                             18,
                             20,
                             21,
                             24,
                             25,
                             45,
                             48,
                             49,
                             59,
                             60,
                             66,
                             67,
                             68,
                             75,
                             82,
                             84,
                             85,
                             101,
                             118,
                             147,
                             171,
                             173,
                             213]},
                   {'comment': '#8,18,38,42,69,70# no activity '
                               '<21,60,67,68,75,84,85>; #89# low activity <118>; '
                               '#52# reaction is extremly weak <82>; #8# anodic '
                               'enzyme form shows no activity <18>; #12# no '
                               'activity at pH 7.5, slight activity at pH 10.8 '
                               '<45>; #5# weak activity with isoenzyme A2, no '
                               'activity with isoenzyme B2 and C2 <48>; #9# '
                               'oxidized with ADH-3, no activity with ADH-1 and '
                               'ADH-2 <49>; #8# class I isoenzymes <13>; #8# no '
                               'activity with isoenzyme beta3,beta3 <20>; #80# '
                               'reaction is catalyzed by the pyrazole-sensitive '
                               'enzyme, no activity with the pyrazole-insensitive '
                               'enzyme <24>; #43# reaction is catalyzed by the '
                               'cathodic pyrazole-sensitive enzyme, no activity by '
                               'the cathodic pyrazole-insensitive enzyme and by '
                               'the anodic pyrazole-insensitive enzyme <25>; #8# '
                               'activity detected with class II isoenzyme pi-ADH '
                               '<14>; #8# oxidized by isoenzyme beta1,beta1 <20>; '
                               '#8# class III isoenzyme chi-ADH shows no activity '
                               '<16>; #8# no activity with class III enzyme <11>; '
                               '#112# 49.9% activity compared to ethanol <213>) {r',
                    'data': 'methanol + NAD+ = formaldehyde + NADH + H+',
                    'refs': [11,
                             12,
                             13,
                             14,
                             16,
                             18,
                             20,
                             21,
                             24,
                             25,
                             45,
                             48,
                             49,
                             59,
                             60,
                             66,
                             67,
                             68,
                             75,
                             82,
                             84,
                             85,
                             101,
                             118,
                             147,
                             171,
                             173,
                             213]},
                   {'comment': '#18# no activity <75>; #5# oxidized by isoenzyme '
                               'A2 and C2 no activity with isoenzyme B2 <48>; #9# '
                               'oxidation with isoenzyme ADH-1 and ADH-3, no '
                               'activity with isoenzyme ADH-2 <49>',
                    'data': 'benzyl alcohol + NAD+ = benzaldehyde + NADH',
                    'refs': [13,
                             14,
                             16,
                             42,
                             47,
                             48,
                             49,
                             60,
                             66,
                             70,
                             75,
                             96,
                             110,
                             147]},
                   {'comment': '#18# no activity <75>; #5# oxidized by isoenzyme '
                               'A2 and C2 no activity with isoenzyme B2 <48>; #9# '
                               'oxidation with isoenzyme ADH-1 and ADH-3, no '
                               'activity with isoenzyme ADH-2 <49>) {r',
                    'data': 'benzyl alcohol + NAD+ = benzaldehyde + NADH',
                    'refs': [13,
                             14,
                             16,
                             42,
                             47,
                             48,
                             49,
                             60,
                             66,
                             70,
                             75,
                             96,
                             110,
                             147]},
                   {'comment': '#18# no activity <75>; #5# oxidized by isoenzyme '
                               'A2, no activity with isoenzymes B2 and C2 <48>; '
                               '#43# reaction is catalyzed by the cathodic '
                               'pyrazole-sensitive enzyme, no activity with the '
                               'cathodic pyrazole-insensitive enzyme and by the '
                               'anodic pyrazole-insensitive enzyme <25>',
                    'data': 'cyclohexanol + NAD+ = cyclohexanone + NADH',
                    'refs': [13, 14, 25, 47, 48, 49, 60, 61, 75, 77, 78, 95, 101]},
                   {'comment': '#70# weak activity <84>; #42# activity with ADH I, '
                               'no activity with ADH II <68>',
                    'data': 'octan-1-ol + NAD+ = n-octanal + NADH',
                    'refs': [11, 13, 14, 21, 25, 48, 49, 60, 68, 75, 84, 85, 101]},
                   {'comment': '#13# broad substrate specificity <126>; #10# '
                               'constitutive enzyme <94>; #42# key enzyme in '
                               'ethanol production <68>; #52# one constitutive '
                               'enzyme, ADH-MI and one inducible enzyme, ADH-MII '
                               '<82>; #53# enzyme may be involved in the '
                               'metabolism of dietary wax esters in salmonid fish '
                               '<59>; #79# the enzyme oxidizes alcohols to '
                               'aldehydes or ketones both for detoxification and '
                               'metabolic purposes <38>; #36# involvement in the '
                               'development of male hamster reproductive system '
                               '<47>; #89# enzyme shows high substrate specificity '
                               'towards primary aliphatic alcohols, no activity '
                               'with 2-butanol, tert-butanol, isoamyl alcohol, '
                               'isobutyl alcohol, 1,6-hexadiol, and mono-, di-, '
                               'and triethanolamine <118>; #91# no activity with '
                               'methanol, 2-propanol, and isoamyl alcohol <105>; '
                               '#10# substrate specificity and stereospecificity, '
                               'substrate binding pocket structure of the 3 '
                               'isozymes, involving Met294, Trp57, and Trp93 '
                               '<120>; #61# substrate specificity of the 2 '
                               'isozmyes with various substrates, overview, '
                               'isozymes are highly specific for the '
                               '(R)-stereoisomers and enantioselctive for the '
                               'R(-)isomers <113>; #106# the enzyme undergoes a '
                               'substantial conformational change in the apo-holo '
                               'transition, accompanied by loop movements at the '
                               'domain interface <108>; #60# alcohol dehydrogenase '
                               'activity may not limit alcohol supply for ester '
                               'production during ripening <146>; #54# Cm-ADH2 '
                               'cannot reduce branched aldehydes <151>; #10# '
                               'effects of pressure on deuterium isotope effects '
                               'of yeast alcohol dehydrogenase using alternative '
                               'substrates <139>; #93# no activity with methanol '
                               '<144>; #94# the enzyme does not act on short-chain '
                               'normal alkyl alcohols, including methanol and '
                               'ethanol <137>; #97# no activity towards methanol, '
                               'ethanol, 1-propanol, triethylene glycol, '
                               'polyethylene glycol 400, polyethylene glycol 1000, '
                               'D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, '
                               'propionaldehyde, butyraldehyde, and valeraldehyde '
                               '<156>; #99# ADH1 preferrs primary alcohols '
                               'containing C3-C8 carbons to secondary alcohols '
                               'such as 2-propanol and 2-butanol. ADH1 possesses '
                               'specific carboxylate ester-forming activity <172>; '
                               '#102# no activity detected with: '
                               'N-benzyl-2-pyrrolidinone, 2-pyrrolidinone, '
                               '3-hexanone, 4-hydroxy-2-butanone, '
                               '(R)-N-benzyl-3-pyrrolidinol, ethanol, '
                               '1,3-propanediol, 1-butanol, 1,4-butanediol, '
                               '1,2,3-butanetriol, 1,2,4-butanetriol, acetol, '
                               '2-phenyl-1-propanol, 3-phenyl-1-propanol, benzyl '
                               'alcohol and glycerol. No activity with NADP+ or '
                               'NADPH <185>; #6# preference for reduction of '
                               'aromatic ketones and alpha-keto esters, and poor '
                               'activity on aromatic alcohols and aldehydes <169>; '
                               '#26# when NADH is replaced with NADPH, the '
                               'reaction rate is reduced by 0.6% <188>; #41# '
                               'activity is severely reduced towards aliphatic '
                               'alcohols of more than 8 carbon atoms for the free '
                               'enzyme, but not so with immobilized HLAD, '
                               'exhibiting an activity towards C22 and C24 '
                               'aliphatic alcohols higher than 50% of the highest '
                               'value, obtained with C8 <204>; #8# differences in '
                               'the activities of total ADH and class I ADH '
                               'isoenzyme between cancer liver tissues and healthy '
                               'hepatocytes may be a factor in ethanol metabolism '
                               'disorders, which can intensify carcinogenesis '
                               '<180>; #113# TADH is a NAD(H)-dependent enzyme and '
                               'shows a very broad substrate spectrum producing '
                               'exclusively the (S)-enantiomer in high '
                               'enantiomeric excess (more than 99%) during '
                               'asymmetric reduction of ketones <197>; #107# '
                               '1-octanal is no substrate for isozyme ADH1C <214>; '
                               '#107# 1-octanal is no substrate for isozyme ADH2 '
                               '<214>; #110# 1-octanal is no substrate for isozyme '
                               'ADH4 <214>; #113# ADH exhibits a clear preference '
                               'for primary alcohols and corresponding aldehydes '
                               'for aliphatic substrates, in the oxidative '
                               'direction activity steeply increases with chain '
                               'length until 1-propanol and then decreases '
                               'slightly again with growing chain length, '
                               'alpha,beta-unsaturated ketones like 3-penten-2-one '
                               'and cyclohexenone are not converted by ADH, almost '
                               'no conversion of methanol (0.2%) and (+)-carvone '
                               '(0.4%) is detected <197>; #122# no activity is '
                               'detected using 1 mM NADP+ <211>; #111# no activity '
                               'towards methanol <210>; #115# substrates are a '
                               'broad range of alkyl alcohols from ethanol to '
                               '1-triacontanol <215>; #124# the physiological '
                               'direction of the catalytic reaction is reduction '
                               'rather than oxidation <219>; #125# the enzyme '
                               'displays a preference for the reduction of '
                               'alicyclic, bicyclic and aromatic ketones and '
                               'alpha-ketoesters, but is poorly active on '
                               'aliphatic, cyclic and aromatic alcohols, showing '
                               'no activity on aldehydes <218>; #124# the enzyme '
                               'shows no activity on aliphatic linear and branched '
                               'alcohols, except for a poor activity on '
                               '2-propyn-1-ol, 3-methyl-1-butanol and 2-pentanol; '
                               'however, it shows a discrete activity on aliphatic '
                               'cyclic and bicyclic alcohols. Benzyl alcohol and '
                               '4-bromobenzyl alcohol are not found to be '
                               'substrates. The S and R enantiomers of '
                               'a-(trifluoromethyl)benzyl alcohol and methyl and '
                               'ethyl mandelates show no apparent activity with '
                               'SaADH. The enzyme shows poor activity on '
                               '(+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol '
                               'and the two enantiomers of 1-(2-naphthyl)ethanol. '
                               'The enzyme is not active on aliphatic and aromatic '
                               'aldehydes, and on aliphatic linear, branched and '
                               'cyclic ketones except for 3-methylcyclohexanone. '
                               'Catalytic inactivity is observed with acetophenone '
                               'and (S)-a-(trifluoromethyl)benzyl <219>; #128# '
                               'methanol, formaldehyde, and acetone are no '
                               'substrates for HpADH3 <222>; #48# no activity with '
                               'methanol, 1-butanol, glycerol or 2-propanol <223>; '
                               '#129# substrate specificity and '
                               'enantiospecificity, overview. The (R)-specific '
                               'alcohol dehydrogenase requires NADH and reduces '
                               'various kinds of carbonyl compounds, including '
                               'ketones and aldehydes. AFPDH reduces '
                               'acetylpyridine derivatives, beta-keto esters, and '
                               'some ketones compounds with high '
                               'enantiospecificity, overview. No activity with '
                               '2-chlorobenzaldehyde and 2-tetralone, poor '
                               'activity with 1-tetralone, pyruvate, '
                               '2-oxobutyrate, oxalacetate, cyclopentanone, '
                               'cyclohexanone, cycloheptanone, and dipropylketone. '
                               'No activity with 1,2-propanediol, '
                               '3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol, '
                               'glycerol, 1-pentanol, poor activity with '
                               '1-butanol, 1-propanol, ethanol, and methanol '
                               '<225>; #86# the enzyme exhibits broad substrate '
                               'specificity towards aliphatic ketones, '
                               'cycloalkanones, aromatic ketones, and ketoesters '
                               '<226>; #133# the enzyme shows broad substrate '
                               'specificity and prefers aliphatic alcohols and '
                               'ketones. There are no large differences in the '
                               'reactivities between primary and secondary '
                               'alcohols. The enzyme produces (S)-alcohols from '
                               'the corresponding ketones. The values of the '
                               'enantiomeric excess increase with the increase of '
                               'chain length except for the reduction of '
                               '2-hexanone. The highest enantioselectivity is '
                               'shown with the reduction of 2-nonanone <239>; '
                               '#134# the NAD+-dependent HvADH1 shows a preference '
                               'for short-chain alcohols, no activity with '
                               'methanol <237>; #144# broad substrate specificity '
                               'with a preference for the reduction of ketones and '
                               'the oxidation of secondary alcohols <138>; #125# '
                               'enzyme displays a preference for the reduction of '
                               'alicyclic, bicyclic and aromatic ketones and '
                               'alpha-keto esters, but is poorly active on '
                               'aliphatic, cyclic and aromatic alcohols, and shows '
                               'no activity on aldehydes <219>; #150# enzyme '
                               'reduces aldehydes to (R)-alcohols with more than '
                               '99.8% enantiomeric excess <243>; #151# enzyme '
                               'selectively reduces the C=O bond of allylic '
                               'aldehydes/ketones to the corresponding '
                               'alpha,beta-unsaturated alcohols and also has the '
                               'capacity of stereoselectively reducing aromatic '
                               'ketones to (S)-enantioselective alcohols. The '
                               'enzyme preferentially catalyzes oxidation of '
                               'allylic/benzyl aldehydes <244>; #71# ethanol '
                               'dehydrogenase activity of Thermoanaerobium brockii '
                               'is both NAD and NADP linked, reversible, and not '
                               'inhibited by low levels of reaction products '
                               '<103>; #120,143# mutation at the substrate-binding '
                               'site, or at a dimer interface, alters kinetic '
                               'properties and protein oligomeric structure, '
                               'active site flexibility is correlated with subunit '
                               'interactions 20 A away <260>; #6# the enzyme '
                               'transfers the pro-S hydrogen of [4R-(2)H]NADH and '
                               'exhibits Prelog specificity <269>; #41# acycloNAD+ '
                               'i.e. NAD+-analogue, where the nicotinamide ribosyl '
                               'moiety has been replaced by the nicotinamide '
                               '(2-hydroxyethoxy)methyl moiety. There is no '
                               'detectable reduction of acycloNAD+ by secondary '
                               'alcohols although these alcohols serve as '
                               'competitive inhibitors. AcycloNAD+ converts horse '
                               'liver ADH from a broad spectrum alcohol '
                               'dehydrogenase, capable of utilizing either primary '
                               'or secondary alcohols, into an exclusively primary '
                               'alcohol dehydrogenase <275>; #51# bifunctional '
                               'enzyme consisting of an N-terminal acetaldehyde '
                               'dehydrogenase (ALDH) and a C-terminal alcohol '
                               'dehydrogenase (ADH). The specificity constant '
                               '(kcat/Km) is 47fold higher for acetaldehyde '
                               'reductase than that for ethanol dehydrogenase '
                               '<279>; #153# enzyme is an alcohol dehydrogenase '
                               'with additional activity for all-trans-retinol, '
                               'reaction of EC 1.1.1.184 <272>; #155# enzyme shows '
                               'activity as a reductase specific for (S)-acetoin, '
                               'EC 1.1.1.76, and both diacetyl reductase (EC '
                               '1.1.1.304) and NAD+-dependent alcohol '
                               'dehydrogenase (EC 1.1.1.1) activities <271>; #160# '
                               'the enzyme additionally catalyzes selective '
                               'reduction of 3-quinuclidinone to '
                               '(R)-3-quinuclidinol, with 84% ee and 62% '
                               'conversion after 22 h <274>; #162# Candida '
                               'albicans ADH1 is a bifunctional enzyme that '
                               'catalyzes methylglyoxal oxidation and reduction, '
                               'cf. EC 1.2.1.23 <287>; #161# the enzyme catalyzes '
                               'NAD(H)-dependent oxidation of various alcohols and '
                               'reduction of aldehydes, with a marked preference '
                               'for substrates with functional group at the '
                               'terminal carbon atom <286>; #166# almost no '
                               'activity with D-arabinonate, D-lyxonate, '
                               'D-galactonate, glycerol, meso-erythritol, '
                               'D-ribitol, D-arabitol, D-xylitol, and D-mannitol. '
                               'No activity with propanal, butanal, hexanal, and '
                               '4-oxobutanoic acid <292>; #165# the enzyme '
                               'catalyzes the reduction of acetophenone '
                               'derivatives to the corresponding (S)-chiral '
                               'alcohols in an enantiomerically pure form. The '
                               'substituents on the benzene ring of the aryl '
                               'ketones exert some effect on the enzyme activity, '
                               'although the influence is not dramatic. The '
                               'enantioselectivity of the reduction is not '
                               'affected by the substituents and pattern of the '
                               'substitution. The alpha-chlorinated acetophenone '
                               'shows a much higher activity than the '
                               'unsubstituted one (more than 10 times) <294>',
                    'data': 'more = ?',
                    'refs': [38,
                             47,
                             59,
                             68,
                             82,
                             94,
                             103,
                             105,
                             108,
                             113,
                             118,
                             120,
                             126,
                             137,
                             138,
                             139,
                             144,
                             146,
                             151,
                             156,
                             169,
                             172,
                             180,
                             185,
                             188,
                             197,
                             204,
                             210,
                             211,
                             214,
                             215,
                             218,
                             219,
                             222,
                             223,
                             225,
                             226,
                             237,
                             239,
                             243,
                             244,
                             260,
                             269,
                             271,
                             272,
                             274,
                             275,
                             279,
                             286,
                             287,
                             292,
                             294]},
                   {'comment': '#8# substrate of isozyme ADH4 <194>) {r',
                    'data': '(2E)-4-hydroxynon-2-enal + NADH + H+ = '
                            '(2E)-non-2-ene-1,4-diol + NAD+',
                    'refs': [194]},
                   {'data': '16-hydroxyhexadecanoate + NAD+ = 16-oxohexadecanoic '
                            'acid + NADH',
                    'refs': [13, 14]},
                   {'data': '17beta-hydroxyetiocholan-3-one + NAD+ = '
                            'ethiocholan-3,17-dione + NADH',
                    'refs': [16]},
                   {'data': '2-deoxy-D-ribose + NAD+ = ? + NADH', 'refs': [14]},
                   {'data': '3,4-dihydro-retinol + NAD+ = 3,4-dihydro-retinal {r}',
                    'refs': [107]},
                   {'data': '3-phenyl-1-propanol + NAD+ = 3-phenyl-1-propanone + '
                            'NADH',
                    'refs': [13, 14]},
                   {'data': '3-pyridylcarbinol + NAD+ = pyridine-3-carbaldehyde + '
                            'NADH',
                    'refs': [18]},
                   {'data': '4-hydroxy-retinol + NAD+ = 4-oxo-retinal + NADH {r}',
                    'refs': [107]},
                   {'comment': '#8# fluorogenic substrate of class I and II '
                               'isozymes <229>',
                    'data': '4-methoxy-1-naphthaldehyde + NAD+ = '
                            '4-methoxy-1-naphthol + NADH + H+',
                    'refs': [229]},
                   {'comment': '#8# substrate for class I ADH <180>',
                    'data': '4-methoxy-1-naphthaldehyde + NAD+ = '
                            '4-methoxy-1-naphthyl alcohol + NADH + H+',
                    'refs': [180]},
                   {'comment': '#8# substrate for class I ADH <206>) {r',
                    'data': '4-methoxy-1-naphthaldehyde + NADH + H+ = '
                            '4-methoxynaphthalene-1-carbaldehyde + NAD+',
                    'refs': [206]},
                   {'comment': '#8# photometric assay substrate <229>',
                    'data': '4-nitrosodimethylaniline + NAD+ = ? + NADH + H+',
                    'refs': [229]},
                   {'comment': '#8# low activity <116>',
                    'data': '5alpha-pregnan-3beta-ol-20-one + NAD+ = '
                            '5alpha-pregnan-3,20-dione + NADH',
                    'refs': [116]},
                   {'comment': '#8# low activity <116>',
                    'data': '5beta-cholanic acid-3-one + NADH = 5beta-cholanic '
                            'acid-3-ol + NAD+',
                    'refs': [116]},
                   {'data': '5beta-pregnan-3,20-dione + NADH = ?', 'refs': [116]},
                   {'data': '5beta-pregnan-3beta-ol-20-one + NAD+ = '
                            '5beta-pregnan-3,20-dione + NADH',
                    'refs': [116]},
                   {'comment': '#8# substrate for class II ADH <206>) {r',
                    'data': '6-methoxy-2-naphthaldehyde + NADH + H+ = '
                            '(6-methoxynaphthalen-2-yl)methanol + NAD+',
                    'refs': [206]},
                   {'comment': '#8# substrate for class II ADH <180>',
                    'data': '6-methoxy-2-naphthaldehyde + NADH + H+ = '
                            '6-methoxy-2-naphthyl alcohol + NAD+',
                    'refs': [180]},
                   {'comment': '#8# class II isozyme, reductive activity <229>',
                    'data': '6-methoxy-2-naphthaldehyde + NADH + H+ = '
                            '6-methoxy-2-naphtol + NAD+',
                    'refs': [229]},
                   {'data': 'digitose + NAD+ = ? + NADH', 'refs': [16]},
                   {'data': 'hexanol + NAD+ = hexanal + NADH', 'refs': [119]},
                   {'data': 'isobutyl alcohol + NAD+ = ? + NADH', 'refs': [20]},
                   {'data': 'isobutyramide + NAD+ = ? {r}', 'refs': [124]},
                   {'data': 'isopentenyl alcohol + NAD+ = isopentanone + NADH',
                    'refs': [20]},
                   {'comment': '#8# substrate of class IV ADH <180>',
                    'data': 'm-nitrobenzaldehyde + NAD+ = m-nitrobenzyl alcohol + '
                            'NADH + H+',
                    'refs': [180]},
                   {'data': 'n-butanol + NAD+ = butylaldehyde + NADH + H+',
                    'refs': [180, 206]},
                   {'data': 'n-butanol + NAD+ = butylaldehyde + NADH + H+ {r}',
                    'refs': [180, 206]},
                   {'comment': '#8# substrate of isozyme ADH4 <194>) {r',
                    'data': 'p-nitrobenzaldehyde + NADH + H+ = p-nitrobenzyl '
                            'alcohol + NAD+',
                    'refs': [194]},
                   {'data': 'phenylalaninol + NAD+ = ? + NADH', 'refs': [16]},
                   {'comment': '#8# substrate of isozyme ADH4 <194>) {r',
                    'data': 'retinal + NADH + H+ = retinol + NAD+',
                    'refs': [194]},
                   {'data': 'retinol + NAD+ = retinal + NADH', 'refs': [115]},
                   {'data': 'trans-4-(N,N-dimethylamino)-cinnamaldehyde + NADH = '
                            'trans-4-(N,N-dimethylamino)-cinnamyl alcohol + NAD+',
                    'refs': [19]},
                   {'data': 'tryptophol + NAD+ = ? + NADH', 'refs': [14]},
                   {'data': 'vanillyl alcohol + NAD+ = vanillin + NADH',
                    'refs': [14, 16]},
                   {'data': 'n-butanol + NAD+ = n-butanal + NADH',
                    'refs': [120, 186]},
                   {'data': 'n-butanol + NAD+ = n-butanal + NADH {r}',
                    'refs': [120, 186]},
                   {'comment': '#97# 100% activity <156>; #47# 199% of the '
                               'activity with 2-phenylethanol <149>; #113# 47% '
                               'activity compared to cyclohexanol <197>; #133# '
                               'i.e. phenylmethanol <239>) |#113# 154% activity '
                               'compared to cyclohexanone <197>; #113# 178% '
                               'activity compared to cyclohexanone <197>; #120# '
                               '33% of the activity with butan-2-ol <256>',
                    'data': 'benzyl alcohol + NAD+ = benzaldehyde + NADH + H+',
                    'refs': [147,
                             149,
                             153,
                             154,
                             156,
                             159,
                             165,
                             180,
                             197,
                             202,
                             205,
                             207,
                             239,
                             256,
                             257,
                             260]},
                   {'comment': '#97# 100% activity <156>; #47# 199% of the '
                               'activity with 2-phenylethanol <149>; #113# 47% '
                               'activity compared to cyclohexanol <197>; #133# '
                               'i.e. phenylmethanol <239>) |#113# 154% activity '
                               'compared to cyclohexanone <197>; #113# 178% '
                               'activity compared to cyclohexanone <197>; #120# '
                               '33% of the activity with butan-2-ol <256>| {r',
                    'data': 'benzyl alcohol + NAD+ = benzaldehyde + NADH + H+',
                    'refs': [147,
                             149,
                             153,
                             154,
                             156,
                             159,
                             165,
                             180,
                             197,
                             202,
                             205,
                             207,
                             239,
                             256,
                             257,
                             260]},
                   {'comment': '#144# 38% of the activity with acetoin <138>',
                    'data': 'cyclohexanone + NADH + H+ = cyclohexanol + NAD+',
                    'refs': [116, 138, 218]},
                   {'comment': '#144# 38% of the activity with acetoin <138>) {r',
                    'data': 'cyclohexanone + NADH + H+ = cyclohexanol + NAD+',
                    'refs': [116, 138, 218]},
                   {'comment': '#8# class IV isozyme, reductive activity <229>',
                    'data': '3-nitrobenzaldehyde + NADH + H+ = 3-nitrobenzyl '
                            'alcohol + NAD+',
                    'refs': [225, 229]},
                   {'comment': '#8# class IV isozyme, reductive activity <229>) {r',
                    'data': '3-nitrobenzaldehyde + NADH + H+ = 3-nitrobenzyl '
                            'alcohol + NAD+',
                    'refs': [225, 229]},
                   {'comment': '#97# 30% activity compared to benzyl alcohol '
                               '<156>; #31# 15.7% of the activity with ethanol '
                               '<181>; #99# about 80% of activity with ethanol, '
                               'ADH1 <172>; #113# 142% activity compared to '
                               'cyclohexanol <197>; #112# 67.7% activity compared '
                               'to ethanol <213>',
                    'data': '1-butanol + NAD+ = butanal + NADH + H+',
                    'refs': [144,
                             147,
                             156,
                             172,
                             181,
                             197,
                             207,
                             210,
                             213,
                             222,
                             223,
                             229,
                             239,
                             286]},
                   {'comment': '#97# 30% activity compared to benzyl alcohol '
                               '<156>; #31# 15.7% of the activity with ethanol '
                               '<181>; #99# about 80% of activity with ethanol, '
                               'ADH1 <172>; #113# 142% activity compared to '
                               'cyclohexanol <197>; #112# 67.7% activity compared '
                               'to ethanol <213>) {r',
                    'data': '1-butanol + NAD+ = butanal + NADH + H+',
                    'refs': [144,
                             147,
                             156,
                             172,
                             181,
                             197,
                             207,
                             210,
                             213,
                             222,
                             223,
                             229,
                             239,
                             286]},
                   {'data': '(S)-2-butanol + NAD+ = butanone + NADH + H+ {r}',
                    'refs': [31, 53]},
                   {'comment': '#8# low activity <116>',
                    'data': '5beta-androstan-17beta-ol-3-one + NAD+ = '
                            '5beta-androstan-3,17-dione + NADH',
                    'refs': [116]},
                   {'data': '5beta-androstan-3beta-ol-17-one + NAD+ = '
                            '5beta-androstan-3,17-dione + NADH',
                    'refs': [116]},
                   {'comment': '#70# weak activity <84>; #41# (R)-2-octanol and '
                               '(S)-2-octanol <31>',
                    'data': 'octan-2-ol + NAD+ = octan-2-one + NADH',
                    'refs': [16, 31, 61, 84]},
                   {'comment': '#42# activity with ADH I, no activity with ADH II '
                               '<68>',
                    'data': 'furfuryl alcohol + NAD+ = furfural + NADH',
                    'refs': [16, 68]},
                   {'comment': '#42# activity with ADH I, no activity with ADH II '
                               '<68>) {r',
                    'data': 'furfuryl alcohol + NAD+ = furfural + NADH',
                    'refs': [16, 68]},
                   {'data': '5alpha-androstan-17beta-ol-3-one + NADH + H+ = '
                            '3beta,17beta-dihydroxy-5alpha-androstan + NAD+',
                    'refs': [51, 116]},
                   {'comment': '#8# substrate of class IV ADH isozyme <206>',
                    'data': 'm-nitrobenzaldehyde + NADH + H+ = m-nitrobenzyl '
                            'alcohol + NAD+',
                    'refs': [49, 206]},
                   {'comment': '#8# substrate of class IV ADH isozyme <206>) {r',
                    'data': 'm-nitrobenzaldehyde + NADH + H+ = m-nitrobenzyl '
                            'alcohol + NAD+',
                    'refs': [49, 206]},
                   {'comment': '#42# activity with ADH I, no activity with ADH II '
                               '<68>',
                    'data': 'pentanol + NAD+ = n-pentanal + NADH',
                    'refs': [11, 45, 49, 60, 61, 68, 69, 71, 75, 77, 78, 85]},
                   {'comment': '#36# oxidized at pH 10, not oxidized at pH 7.5 '
                               '<47>',
                    'data': '12-hydroxydodecanoate + NAD+ = 12-oxododecanoic acid '
                            '+ NADH',
                    'refs': [11, 14, 16, 47, 49, 53, 60, 95, 96]},
                   {'data': 'octanal + NADH + H+ = octanol + NAD+',
                    'refs': [16, 49, 60]}]),
                 ('SS',
                  [{'data': '(4°C, 10 mM HEPES buffer, 1 mM dithioerythritol, pH '
                            '7.5, stable for 2 weeks)',
                    'refs': [16]},
                   {'data': '(4°C, 5 mM Na phosphate, pH 7.5, the half-life is 24 '
                            'h. 0.01 mM ethanol effectively stabilizes for several '
                            'weeks)',
                    'refs': [18]},
                   {'data': '(4°C, 5 mM Na-phosphate, pH 7.5, 50% loss of activity '
                            'after 1 day. Enzyme can be stabilized for up to 2 '
                            'weeks by storage in buffer containing 10 mM ethanol)',
                    'refs': [23]},
                   {'data': '(4°C, pH 7.5, stable for 2-3 weeks)', 'refs': [14]}]),
                 ('ST',
                  [{'bto': 'BTO:0000759',
                    'comment': '#5# isoenzyme A2 and B2 <48>; #36# isoenzyme '
                               'AA-ADH and BB-ADH most abundant in <95>; #8# '
                               'isozyme ADH1C*2 <116>; #9# females show 70% higher '
                               'hepatic alcohol dehydrogenase activity and display '
                               '60% lower voluntary ethanol intake than males. '
                               'Following ethanol administration (1 g/kg ip), '
                               'females generate a transient blood acetaldehyde '
                               'increase with levels that are 2.5fold greater than '
                               'in males. Castration of males leads to an increase '
                               'alcohol dehydrogenase activity the appearance of '
                               'an acetaldehyde burst a reduction of voluntary '
                               'ethanol intake comparable with that of females '
                               '<167>; #8# the activities of total alcohol '
                               'dehydrogenase, aldehyde dehydrogenase and class I '
                               'alcohol dehydrogenase isoenzyme between cancer '
                               'liver tissues and healthy hepatocytes might be a '
                               'factor in ethanol metabolism disorders which can '
                               'intensify carcinogenesis <186>; #107# isozymes '
                               'ADH1C and ADH3 <214>; #8# most abundant in the '
                               'liver <180>; #8# the total alcohol dehydrogenase '
                               'activity is significantly higher in cancer tissues '
                               'than in healthy liver <194>; #132# class III ADH '
                               '<227>',
                    'data': 'liver',
                    'refs': [1,
                             2,
                             5,
                             10,
                             12,
                             13,
                             14,
                             15,
                             16,
                             17,
                             18,
                             19,
                             20,
                             21,
                             22,
                             23,
                             24,
                             25,
                             26,
                             27,
                             28,
                             29,
                             30,
                             31,
                             32,
                             33,
                             34,
                             35,
                             36,
                             37,
                             39,
                             40,
                             41,
                             42,
                             44,
                             45,
                             46,
                             48,
                             49,
                             51,
                             52,
                             54,
                             55,
                             59,
                             60,
                             86,
                             92,
                             93,
                             95,
                             98,
                             101,
                             111,
                             116,
                             117,
                             143,
                             167,
                             175,
                             178,
                             180,
                             186,
                             194,
                             198,
                             200,
                             201,
                             204,
                             205,
                             212,
                             214,
                             224,
                             227,
                             275]},
                   {'bto': 'BTO:0000575',
                    'comment': '#8# the activities of total alcohol dehydrogenase, '
                               'aldehyde dehydrogenase and class I alcohol '
                               'dehydrogenase isoenzyme between cancer liver '
                               'tissues and healthy hepatocytes might be a factor '
                               'in ethanol metabolism disorders which can '
                               'intensify carcinogenesis <186>',
                    'data': 'hepatocyte',
                    'refs': [117, 186]},
                   {'bto': 'BTO:0001175',
                    'comment': '#5,8# isozyme ADH4 <119>',
                    'data': 'retina',
                    'refs': [119]},
                   {'bto': 'BTO:0001307',
                    'comment': '#5# isoenzyme C2 <48>; #8# stomach mucosa, '
                               'mue-alcohol dehydrogenase <96>; #8# isozymes ADH5 '
                               'and ADH4, the total alcohol dehydrogenase activity '
                               'is significantly higher in cancer tissues than in '
                               'healthy stomach <194>',
                    'data': 'stomach',
                    'refs': [48, 49, 50, 53, 96, 125, 194]},
                   {'bto': 'BTO:0000604',
                    'data': 'adenocarcinoma cell',
                    'refs': [229]},
                   {'bto': 'BTO:0000135',
                    'comment': '#8# the activity of the class I ADH isoenzyme is '
                               'significantly lower in the wall of aortic aneurysm '
                               'than in healthy aorta <206>',
                    'data': 'aorta',
                    'refs': [206]},
                   {'bto': 'BTO:0000133',
                    'comment': '#8# among all tested classes of ADH isoenzymes, '
                               'only class I has higher activity in serum of '
                               'patients with breast cancer in stage IV. The total '
                               'ADH activity is not significantly higher in '
                               'patients with breast cancer than in healthy '
                               'controls. The changes in activity, especially in '
                               'class I ADH, appear to be caused by isoenzymes '
                               'being released from the organ damaged by '
                               'metastatic disease <150>; #8# the total ADH '
                               'activity is significantly higher (44%) among '
                               'patients with cancer than healthy ones. The '
                               'activity of class I ADH isoenzymes is elevated '
                               'only in the serum of patients with metastatic '
                               'liver cancer. This increase of activity seems to '
                               'be caused by the enzyme released from liver cancer '
                               'cells and primary tumors originating in other '
                               'organs <186>',
                    'data': 'blood serum',
                    'refs': [150, 186]},
                   {'data': 'cervical cancer cell', 'refs': [229]},
                   {'bto': 'BTO:0001613',
                    'comment': '#8# the total alcohol dehydrogenase activity is '
                               'significantly higher in cancer tissues than in '
                               'healthy colorectum <194>',
                    'data': 'colorectum',
                    'refs': [194]},
                   {'bto': 'BTO:0000959',
                    'comment': '#8# isozyme ADH4, the total alcohol dehydrogenase '
                               'activity is significantly higher in cancer tissues '
                               'than in healthy esophagus <194>',
                    'data': 'esophagus',
                    'refs': [194]},
                   {'bto': 'BTO:0000608', 'data': 'hepatoma cell', 'refs': [180]},
                   {'bto': 'BTO:0001239', 'data': 'serum', 'refs': [194]},
                   {'bto': 'BTO:0001253', 'data': 'skin', 'refs': [194]},
                   {'bto': 'BTO:0000286',
                    'comment': '#8# isozyme ADH4 <194>',
                    'data': 'cornea',
                    'refs': [49, 194]},
                   {'bto': 'BTO:0000671',
                    'comment': '#8# isozyme ADH1 <194>; #9# high expression level '
                               'of ADH5 <228>',
                    'data': 'kidney',
                    'refs': [49, 194, 228]},
                   {'bto': 'BTO:0000763',
                    'comment': '#8# isozyme ADH1 <194>',
                    'data': 'lung',
                    'refs': [49, 194]},
                   {'bto': 'BTO:0000988',
                    'comment': '#8# total activity of alcohol dehydrogenase is not '
                               'significantly different in cancer and normal '
                               'cells. The differences between enzymes of drinkers '
                               'and nondrinkers in both cancer and healthy tissue '
                               'are not significant <191>',
                    'data': 'pancreas',
                    'refs': [49, 191]},
                   {'bto': 'BTO:0001424', 'data': 'uterus', 'refs': [49, 229]},
                   {'bto': 'BTO:0001363',
                    'comment': '#8# the class III enzyme contributes by far the '
                               'bulk of the total alcohol dehydrogenase activity '
                               '<11>; #36# isoenzyme TT-ADH is only found in '
                               'testis <95>; #36# activity increases during the '
                               'prepubertal development <47>',
                    'data': 'testis',
                    'refs': [11, 47, 49, 95]}]),
                 ('SU',
                  [{'comment': '#8# x * 42000, SDS-PAGE <14>; #74# x * 28000, '
                               'SDS-PAGE <2>; #1,8,81,132# x * 40000, SDS-PAGE '
                               '<11,44,52,227>; #24# x * 96000, SDS-PAGE <128>; '
                               '#86# x * 30000, SDS-PAGE <226>; #158# x * 85000, '
                               'SDS-PAGE <283>; #14# x * 37500, SDS-PAGE <81>; '
                               '#25# x * 31997, amino acid sequence calculation '
                               '<106>; #99# x * 37443, ADH1, calculated from '
                               'sequence <172>; #15# x * 37983, ADH3, calculated '
                               'from sequence <172>; #31# x * 41300, SDS-PAGE '
                               '<181>; #127# x * 31000, recombinant His6-tagged '
                               'enzyme, SDS-PAGE <231>; #151# x * 36411, '
                               'calculated, x * 37000, SDS-PAGE <244>; #104# x * '
                               '37066, calculated <177>; #105# x * 37311, '
                               'calculated <177>; #73# x * 96000, wild-type, '
                               'SDS-PAGE <241>; #153# x * 40000, SDS-PAGE, x * '
                               '39900, calculated <272>; #158# x * 88000, '
                               'calculated from sequence <283>',
                    'data': '?',
                    'refs': [2,
                             11,
                             14,
                             44,
                             52,
                             81,
                             106,
                             128,
                             172,
                             177,
                             181,
                             226,
                             227,
                             231,
                             241,
                             244,
                             272,
                             283]},
                   {'comment': '#16# 2 * 45000, SDS-PAGE <79>; #26,79# 2 * 28000, '
                               'SDS-PAGE <61,188>; #67,82# 2 * 58000, SDS-PAGE '
                               '<77,78>; #18# 2 * 35000, SDS-PAGE <75>; #44# 2 * '
                               '38000, SDS-PAGE <114>; #8,10,36,53,80# 2 * 40000, '
                               'SDS-PAGE <16,23,24,59,87,95>; #36# 2 * 41000, '
                               'SDS-PAGE <47>; #68# 2 * 42000, SDS-PAGE <69>; #45# '
                               '2 * 46000, SDS-PAGE <6>; #89# 2 * 43000, SDS-PAGE '
                               '<118>; #12# 2 * 36000, SDS-PAGE <45>; #21,46# 2 * '
                               '37000, SDS-PAGE <66,70,72,165>; #42# 2 * 38000, '
                               'enzyme form ADHII, SDS-PAGE <68>; #8# 2 * 41000, '
                               'class III isoenzyme chi ADH, SDS-PAGE <16>; #9# 2 '
                               '* 43000, ADH-1, SDS-PAGE <49>; #8# 2 * 42000, '
                               'anodic enzyme form, SDS-PAGE <18>; #69# 2 * 42000, '
                               'enzyme form ADH-2 and ADH-3, SDS-PAGE <60>; #5# 2 '
                               '* 47000, isoenzyme C2, SDS-PAGE <48>; #5# 2 * '
                               '39000, isoenzyme B2, SDS-PAGE <48>; #9# 2 * 40000, '
                               'ADH-3, SDS-PAGE <49>; #9# 2 * 39000, ADH-2, '
                               'SDS-PAGE <49>; #12# 2 * 41700, enzyme form CM-I: a '
                               'polypeptide chain + C polypeptide chain, enzyme '
                               'form CM-II: B-chain + C-chain, enzyme form CM III, '
                               'homodimer of C chains, SDS-PAGE <46>; #5# 2 * '
                               '43000, isoenzyme A2, SDS-PAGE <48>; #42# 2 * '
                               '40000, enzyme form ADHI <68>; #4,72,76# 2 * 27800, '
                               'SDS-PAGE <64>; #42# 2 * 34700, enzyme form ADH-I, '
                               'SDS-PAGE <67>; #3# 2 * 30000 <4>; #42# 2 * 31100, '
                               'enzyme form ADH-II, SDS-PAGE <67>; #61# 2 * 31000, '
                               'ADH II, SDS-PAGE <113>; #106# dimer of dimers, '
                               'X-ray crystallography <161>; #101# 2 * 36900, '
                               'SDS-PAGE <171>; #44# 2 * 38000, recombinant '
                               'enzyme, SDS-PAGE <232>; #73# 2 * 48600, alcohol '
                               'dehydrogenase domain, SDS-PAGE. Unlike the native '
                               'ADHE, the alcohol dehydrogenase domain alone does '
                               'not assemble into spirosome structures <241>; #20# '
                               '2 * 40700, calculated <284>; #161# 2 * 37555, '
                               'calculated <286>',
                    'data': 'dimer',
                    'refs': [4,
                             6,
                             16,
                             18,
                             21,
                             23,
                             24,
                             45,
                             46,
                             47,
                             48,
                             49,
                             59,
                             60,
                             61,
                             64,
                             66,
                             67,
                             68,
                             69,
                             70,
                             71,
                             72,
                             75,
                             77,
                             78,
                             79,
                             87,
                             95,
                             113,
                             114,
                             118,
                             161,
                             165,
                             171,
                             188,
                             194,
                             205,
                             232,
                             241,
                             284,
                             286]},
                   {'comment': '#27# quaternary organization and stability, '
                               'overview <129>; #8# structure modelling <115>; '
                               '#48# Adh3 forms a Ni2+-containing homodimer in its '
                               'active form, crystal structure analysis, larger '
                               'aggregates are inactive <223>; #125# tetramer '
                               'structure results from chemical crosslinking '
                               'experiments <219>',
                    'data': 'More',
                    'refs': [115, 129, 219, 223]}]),
                 ('SY',
                  [{'comment': '#118# mutant enzyme S109P/L116S/Y294C <193>',
                    'data': 'alcohol dehydrogenase 1',
                    'refs': [190, 193, 212, 228]},
                   {'data': 'ADH',
                    'refs': [108,
                             111,
                             113,
                             115,
                             117,
                             118,
                             119,
                             126,
                             127,
                             129,
                             152,
                             153,
                             154,
                             155,
                             157,
                             158,
                             159,
                             160,
                             161,
                             163,
                             164,
                             194,
                             196,
                             197,
                             199,
                             200,
                             201,
                             203,
                             205,
                             206,
                             207,
                             208,
                             209,
                             211,
                             213,
                             229,
                             231,
                             233,
                             248,
                             251,
                             261,
                             292]},
                   {'data': 'ADH1B', 'refs': [273]},
                   {'data': 'ADH1C*1', 'refs': [116]},
                   {'data': 'ADH1C*2', 'refs': [116]},
                   {'data': 'ALDH', 'refs': [229]},
                   {'data': 'aldehyde dehydrogenase', 'refs': [229]},
                   {'comment': '#8# isoenzyme <206>; #8# isozyme <180>',
                    'data': 'class I ADH',
                    'refs': [180, 206, 229]},
                   {'comment': '#8# isoenzyme <206>; #8# isozyme <180>',
                    'data': 'class II ADH',
                    'refs': [180, 206, 229]},
                   {'data': 'class III ADH', 'refs': [229]},
                   {'comment': '#8# isozyme <180>',
                    'data': 'class IV ADH',
                    'refs': [180, 229]},
                   {'comment': '#10# isozyme <202>',
                    'data': 'ADH1',
                    'refs': [156, 172, 202, 215, 228, 252, 282, 287]},
                   {'comment': '#110# isozyme <214>',
                    'data': 'ADH4',
                    'refs': [124, 174, 177, 214, 252]}]),
                 ('TN',
                  [{'comment': '#8# turnover-numbers for the class I isoenzymes '
                               'with the substrates ethanol, methanol, ethylene '
                               'glycol, benzyl alcohol, octanol, cyclohexanol and '
                               '16-hydroxyhexadecanoic acid <13>; #41# Km-values '
                               'of active-site Co(II)substituted enzyme <31>; '
                               '#4,76# kinetics of ethanol oxidation <63>; #5# '
                               'kcat for isozymes ADH1, and ADH4 for all retinoid '
                               'substrates in forward and reverse reaction <119>; '
                               '#8# kcat for isozymes ADH1B1, ADH1B2, and ADH4 for '
                               'all retinoid substrates in forward and reverse '
                               'reaction <119>; #5# effects of tert-butanol, '
                               'butyramide, valeramide and capronamide on '
                               'turnover-number of ethanol <141>; #23# kinetic '
                               'data füor wild-type enzyme and chimeric enzyme '
                               'created by insertion of an RTX domain from the '
                               'adenylate cyclase of Bordetella pertussis into a '
                               'loop near the catalytic active site of the '
                               'thermostable alcohol dehydrogenase D (AdhD) from '
                               'Pyrococcus furiosus <289>',
                    'data': '-999 {more}',
                    'refs': [13, 28, 31, 63, 119, 141, 289],
                    'units': '1/s'},
                   {'chebi': 'CHEBI:17898',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.018 {all-trans-retinal}',
                    'refs': [107],
                    'substrate': 'all-trans-retinal',
                    'units': '1/s',
                    'value': 0.018},
                   {'chebi': 'CHEBI:17336',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.028 {all-trans-retinol}',
                    'refs': [107],
                    'substrate': 'all-trans-retinol',
                    'units': '1/s',
                    'value': 0.028},
                   {'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.038 {Octanol}',
                    'refs': [115],
                    'substrate': 'Octanol',
                    'units': '1/s',
                    'value': 0.038},
                   {'comment': '#8# recombinant allozyme Val308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.04 {Octanol}',
                    'refs': [115],
                    'substrate': 'Octanol',
                    'units': '1/s',
                    'value': 0.04},
                   {'chebi': 'CHEBI:50211',
                    'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.087 {retinol}',
                    'refs': [115],
                    'substrate': 'retinol',
                    'units': '1/s',
                    'value': 0.087},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.088 {3,4-dihydro-retinol}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinol',
                    'units': '1/s',
                    'value': 0.088},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.092 {4-hydroxy-retinol}',
                    'refs': [107],
                    'substrate': '4-hydroxy-retinol',
                    'units': '1/s',
                    'value': 0.092},
                   {'chebi': 'CHEBI:17790',
                    'data': '0.102 {methanol}',
                    'refs': [12],
                    'substrate': 'methanol',
                    'units': '1/s',
                    'value': 0.102},
                   {'chebi': 'CHEBI:50211',
                    'comment': '#8# recombinant allozyme Val308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.11 {retinol}',
                    'refs': [115],
                    'substrate': 'retinol',
                    'units': '1/s',
                    'value': 0.11},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B1 <107>',
                    'data': '0.167 {4-oxo-retinal}',
                    'refs': [107],
                    'substrate': '4-oxo-retinal',
                    'units': '1/s',
                    'value': 0.167},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# recombinant allozyme Ile308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.167 {ethanol}',
                    'refs': [115],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 0.167},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# recombinant allozyme Val308, pH 7.5, 25°C '
                               '<115>',
                    'data': '0.175 {ethanol}',
                    'refs': [115],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 0.175},
                   {'data': '0.183 {1-Pentanol}',
                    'refs': [11],
                    'substrate': '1-Pentanol',
                    'units': '1/s',
                    'value': 0.183},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.22 {3,4-dihydro-retinal}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinal',
                    'units': '1/s',
                    'value': 0.22},
                   {'data': '0.245 {Pentanol}',
                    'refs': [16],
                    'substrate': 'Pentanol',
                    'units': '1/s',
                    'value': 0.245},
                   {'chebi': 'CHEBI:17336',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.25 {all-trans-retinol}',
                    'refs': [107],
                    'substrate': 'all-trans-retinol',
                    'units': '1/s',
                    'value': 0.25},
                   {'data': '0.333 {12-Hydroxydodecanoic acid}',
                    'refs': [11],
                    'substrate': '12-Hydroxydodecanoic acid',
                    'units': '1/s',
                    'value': 0.333},
                   {'chebi': 'CHEBI:17336',
                    'data': '0.4 {all-trans-retinol}',
                    'refs': [53],
                    'substrate': 'all-trans-retinol',
                    'units': '1/s',
                    'value': 0.4},
                   {'data': '0.467 {Vanillyl alcohol}',
                    'refs': [16],
                    'substrate': 'Vanillyl alcohol',
                    'units': '1/s',
                    'value': 0.467},
                   {'chebi': 'CHEBI:17898',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '0.55 {all-trans-retinal}',
                    'refs': [107],
                    'substrate': 'all-trans-retinal',
                    'units': '1/s',
                    'value': 0.55},
                   {'data': '0.583 {Cyclohexanol}',
                    'refs': [14],
                    'substrate': 'Cyclohexanol',
                    'units': '1/s',
                    'value': 0.583},
                   {'comment': '#8# pH 7.5, anodic enzyme form <18>',
                    'data': '0.667 {Pentanol}',
                    'refs': [18],
                    'substrate': 'Pentanol',
                    'units': '1/s',
                    'value': 0.667},
                   {'comment': '#8# pH 7.5, anodic enzyme form <18>',
                    'data': '0.683 {3-Pyridylcarbinol}',
                    'refs': [18],
                    'substrate': '3-Pyridylcarbinol',
                    'units': '1/s',
                    'value': 0.683},
                   {'comment': '#8# pH 7.5, anodic enzyme form <18>',
                    'data': '0.7 {butanol}',
                    'refs': [18],
                    'substrate': 'butanol',
                    'units': '1/s',
                    'value': 0.7},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# pH 7.5, anodic enzyme form <18>',
                    'data': '0.7 {ethanol}',
                    'refs': [18],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 0.7},
                   {'comment': '#8# pH 7.5, anodic enzyme form <18>',
                    'data': '0.717 {NAD+}',
                    'refs': [18],
                    'substrate': 'NAD+',
                    'units': '1/s',
                    'value': 0.717},
                   {'data': '0.75 {2-propanol}',
                    'refs': [14],
                    'substrate': '2-propanol',
                    'units': '1/s',
                    'value': 0.75},
                   {'chebi': 'CHEBI:30742',
                    'data': '0.75 {ethylene glycol}',
                    'refs': [14],
                    'substrate': 'ethylene glycol',
                    'units': '1/s',
                    'value': 0.75},
                   {'chebi': 'CHEBI:17336',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '0.9 {all-trans-retinol}',
                    'refs': [107],
                    'substrate': 'all-trans-retinol',
                    'units': '1/s',
                    'value': 0.9},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '1.22 {3,4-dihydro-retinal}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinal',
                    'units': '1/s',
                    'value': 1.22},
                   {'chebi': 'CHEBI:17898',
                    'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '1.83 {all-trans-retinal}',
                    'refs': [107],
                    'substrate': 'all-trans-retinal',
                    'units': '1/s',
                    'value': 1.83},
                   {'chebi': 'CHEBI:17890',
                    'data': '1.83 {tryptophol}',
                    'refs': [14],
                    'substrate': 'tryptophol',
                    'units': '1/s',
                    'value': 1.83},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# pH 10.0, anodic enzyme form <18>',
                    'data': '10.2 {ethanol}',
                    'refs': [18],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 10.2},
                   {'data': '16 {Pentanol}',
                    'refs': [53],
                    'substrate': 'Pentanol',
                    'units': '1/s',
                    'value': 16.0},
                   {'data': '17.2 {Propanol}',
                    'refs': [53],
                    'substrate': 'Propanol',
                    'units': '1/s',
                    'value': 17.2},
                   {'data': '19.5 {Hexanol}',
                    'refs': [53],
                    'substrate': 'Hexanol',
                    'units': '1/s',
                    'value': 19.5},
                   {'data': '2.17 {(S)-2-butanol}',
                    'refs': [53],
                    'substrate': '(S)-2-butanol',
                    'units': '1/s',
                    'value': 2.17},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '2.5 {3,4-dihydro-retinol}',
                    'refs': [107],
                    'substrate': '3,4-dihydro-retinol',
                    'units': '1/s',
                    'value': 2.5},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# per active site <12>',
                    'data': '2.5 {ethanol}',
                    'refs': [12],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 2.5},
                   {'data': '2.83 {1-Octanol}',
                    'refs': [11],
                    'substrate': '1-Octanol',
                    'units': '1/s',
                    'value': 2.83},
                   {'chebi': 'CHEBI:28816',
                    'data': '2.83 {2-deoxy-D-ribose}',
                    'refs': [14],
                    'substrate': '2-deoxy-D-ribose',
                    'units': '1/s',
                    'value': 2.83},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '2.83 {4-hydroxy-retinol}',
                    'refs': [107],
                    'substrate': '4-hydroxy-retinol',
                    'units': '1/s',
                    'value': 2.83},
                   {'data': '2.95 {12-hydroxydodecanoate}',
                    'refs': [53],
                    'substrate': '12-hydroxydodecanoate',
                    'units': '1/s',
                    'value': 2.95},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '20 {4-oxo-retinal}',
                    'refs': [107],
                    'substrate': '4-oxo-retinal',
                    'units': '1/s',
                    'value': 20.0},
                   {'data': '3.03 {12-hydroxydodecanoate}',
                    'refs': [16],
                    'substrate': '12-hydroxydodecanoate',
                    'units': '1/s',
                    'value': 3.03},
                   {'chebi': 'CHEBI:17935',
                    'data': '3.33 {octanal}',
                    'refs': [16],
                    'substrate': 'octanal',
                    'units': '1/s',
                    'value': 3.33},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme gamma1,gamma1 <13>',
                    'data': '3.83 {ethanol}',
                    'refs': [13],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 3.83},
                   {'chebi': 'CHEBI:16236',
                    'data': '30.7 {ethanol}',
                    'refs': [53],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 30.7},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH4 <107>',
                    'data': '34.2 {4-hydroxy-retinol}',
                    'refs': [107],
                    'substrate': '4-hydroxy-retinol',
                    'units': '1/s',
                    'value': 34.2},
                   {'data': '34.8 {butanol}',
                    'refs': [53],
                    'substrate': 'butanol',
                    'units': '1/s',
                    'value': 34.8},
                   {'data': '4 {12-hydroxydodecanoate}',
                    'refs': [14],
                    'substrate': '12-hydroxydodecanoate',
                    'units': '1/s',
                    'value': 4.0},
                   {'chebi': 'CHEBI:16236',
                    'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '4 {ethanol}',
                    'refs': [13],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 4.0},
                   {'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '4.33 {Octanol}',
                    'refs': [13],
                    'substrate': 'Octanol',
                    'units': '1/s',
                    'value': 4.33},
                   {'chebi': 'CHEBI:17987',
                    'comment': '#8# isoenzyme alpha,gamma1 <13>',
                    'data': '4.67 {benzyl alcohol}',
                    'refs': [13],
                    'substrate': 'benzyl alcohol',
                    'units': '1/s',
                    'value': 4.67},
                   {'chebi': 'CHEBI:55329',
                    'data': '6.17 {16-hydroxyhexadecanoate}',
                    'refs': [14],
                    'substrate': '16-hydroxyhexadecanoate',
                    'units': '1/s',
                    'value': 6.17},
                   {'data': '7.33 {Octanol}',
                    'refs': [16],
                    'substrate': 'Octanol',
                    'units': '1/s',
                    'value': 7.33},
                   {'chebi': 'CHEBI:88817',
                    'data': '7.5 {3-Phenyl-1-propanol}',
                    'refs': [14],
                    'substrate': '3-Phenyl-1-propanol',
                    'units': '1/s',
                    'value': 7.5},
                   {'comment': '#8# pH 7.5, 25°C, isozyme ADH1B2 <107>',
                    'data': '7.83 {4-oxo-retinal}',
                    'refs': [107],
                    'substrate': '4-oxo-retinal',
                    'units': '1/s',
                    'value': 7.83},
                   {'chebi': 'CHEBI:16236',
                    'data': '7.83 {ethanol}',
                    'refs': [14],
                    'substrate': 'ethanol',
                    'units': '1/s',
                    'value': 7.83},
                   {'data': '8 {Pentanol}',
                    'refs': [14],
                    'substrate': 'Pentanol',
                    'units': '1/s',
                    'value': 8.0},
                   {'data': '8.33 {Octanol}',
                    'refs': [14],
                    'substrate': 'Octanol',
                    'units': '1/s',
                    'value': 8.33},
                   {'data': '8.67 {Vanillyl alcohol}',
                    'refs': [14],
                    'substrate': 'Vanillyl alcohol',
                    'units': '1/s',
                    'value': 8.67},
                   {'chebi': 'CHEBI:17987',
                    'data': '9.17 {benzyl alcohol}',
                    'refs': [14],
                    'substrate': 'benzyl alcohol',
                    'units': '1/s',
                    'value': 9.17}]),
                 ('TO',
                  [{'comment': '#5,8,10# assay at <107,115,119,121,124,229,295>; '
                               '#61# assay at, forward and reverse reaction <113>; '
                               '#10# free enzyme, at 25°C <196>',
                    'data': '25',
                    'refs': [106,
                             107,
                             113,
                             115,
                             119,
                             121,
                             124,
                             131,
                             196,
                             229,
                             295]},
                   {'comment': '#8,41# assay at <116>',
                    'data': '30-37',
                    'refs': [116]}]),
                 ('TS',
                  [{'comment': '#8# unstable at room temperature and above <12>',
                    'data': '23',
                    'refs': [12]},
                   {'comment': '#41# distinct subunits have different deactivation '
                               'properties <37>; #10# effect of salts in the high '
                               'concentration range on the thermal stability '
                               '<148>; #41# alpha-cyclodextrin causes thermal '
                               'stabilization and delays the onset of secondary '
                               'structural unfolding and aggregation by approx. '
                               '10°C and the midpoint temperatures by more than '
                               '5°C. alpha-Cyclodextrin diminishes the '
                               'deactivation of the enzyme, decreasing the '
                               'deactivation constant by more than 50%, and '
                               'clearly reveals the stabilization of the enzyme '
                               'not only structurally but also kinetically at '
                               'higher temperatures <178>; #44# temperature '
                               'stability profiles of recombinantly expressed '
                               'enzymes, overview <232>',
                    'data': '-999',
                    'refs': [37, 112, 115, 148, 178, 232]}]),
                 ('references',
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