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brendapy-0.5.0
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Parsing BRENDA information.
| ویژگی | مقدار |
|---|---|
| سیستم عامل | - |
| نام فایل | brendapy-0.5.0 |
| نام | brendapy |
| نسخه کتابخانه | 0.5.0 |
| نگهدارنده | ['Matthias Koenig'] |
| ایمیل نگهدارنده | ['konigmatt@googlemail.com'] |
| نویسنده | Matthias Koenig |
| ایمیل نویسنده | konigmatt@googlemail.com |
| آدرس صفحه اصلی | https://github.com/matthiaskoenig/brendapy |
| آدرس اینترنتی | https://pypi.org/project/brendapy/ |
| مجوز | LGPL-3.0 |
.. 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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:target: https://github.com/matthiaskoenig/brendapy/workflows/CI-CD
:alt: GitHub Actions CI/CD Status
.. image:: https://img.shields.io/pypi/v/brendapy.svg
:target: https://pypi.org/project/brendapy/
:alt: Current PyPI Version
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:target: https://pypi.org/project/brendapy/
:alt: Supported Python Versions
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:target: http://opensource.org/licenses/LGPL-3.0
:alt: GNU Lesser General Public License 3
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:target: https://codecov.io/gh/matthiaskoenig/brendapy
:alt: Codecov
.. image:: https://zenodo.org/badge/DOI/10.5281/zenodo.3355000.svg
:target: https://doi.org/10.5281/zenodo.3355000
:alt: Zenodo DOI
.. image:: https://img.shields.io/badge/code%20style-black-000000.svg
:target: https://github.com/ambv/black
: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',
{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 '
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201: {'info': 'Bergman, T.; Zhang, K.; Palmberg, C.; Joernvall, '
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202: {'info': 'Pal, S.; Park, D.H.; Plapp, B.V.: Activity of '
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207: {'info': 'Pennacchio, A.; Esposito, L.; Zagari, A.; Rossi, '
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208: {'info': 'Carvalho, E.; Solferini, V.; Matioli, S.: '
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'pubmed': 19120802},
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'pubmed': 3730426},
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'pubmed': 24509923},
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256: {'info': 'Guagliardi, A.; Martino, M.; Iaccarino, I.; De '
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286: {'info': 'Ashraf, R.; Rashid, N.; Kanai, T.; Imanaka, T.; '
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('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',
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195: {'info': 'Peng, H.; Wu, G.; Shao, W.: The aldehyde/alcohol '
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196: {'info': 'Zhao, Q.; Hou, Y.; Gong, G.H.; Yu, M.A.; Jiang, '
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198: {'info': 'Plapp, B.V.: Conformational changes and '
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200: {'info': 'Staab, C.A.; Hellgren, M.; Hoeoeg, J.O.: Medium- '
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'pubmed': 19011746},
201: {'info': 'Bergman, T.; Zhang, K.; Palmberg, C.; Joernvall, '
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202: {'info': 'Pal, S.; Park, D.H.; Plapp, B.V.: Activity of '
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204: {'info': 'Cea, G.; Wilson, L.; Bolivar, J.; Markovits, A.; '
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206: {'info': 'Jelski, W.; Orywal, K.; Panek, B.; Gacko, M.; '
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207: {'info': 'Pennacchio, A.; Esposito, L.; Zagari, A.; Rossi, '
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208: {'info': 'Carvalho, E.; Solferini, V.; Matioli, S.: '
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209: {'info': 'Devi, P.G.; Chakraborty, P.K.; Dasgupta, D.: '
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'pubmed': 15253444},
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229: {'info': 'Orywal, K.; Jelski, W.; Zdrodowski, M.; '
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233: {'info': 'Komatsu, S.; Deschamps, T.; Thibaut, D.; Hiraga, '
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234: {'info': 'Pennacchio, A.; Rossi, M.; Raia, C.A.: Synthesis '
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'pubmed': 16233615},
243: {'info': 'Wu, X.; Zhang, C.; Orita, I.; Imanaka, T.; '
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244: {'info': 'Ying, X.; Wang, Y.; Xiong, B.; Wu, T.; Xie, L.; '
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'pubmed': 24509923},
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252: {'info': 'Liang, J.J.; Zhang, M.L.; Ding, M.; Mai, Z.M.; '
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254: {'info': 'Kontani, A.; Masuda, M.; Matsumura, H.; '
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256: {'info': 'Guagliardi, A.; Martino, M.; Iaccarino, I.; De '
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257: {'info': 'Meadows, C.W.; Tsang, J.E.; Klinman, J.P.: '
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272: {'info': 'Hong, S.H.; Ngo, H.P.; Kang, L.W.; Oh, D.K.: '
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286: {'info': 'Ashraf, R.; Rashid, N.; Kanai, T.; Imanaka, T.; '
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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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19: {'info': 'Schneider-Bernloehr, H.; Formicka-Kozlowska, G.; '
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'pubmed': 2819035},
21: {'info': 'Pares, X.; Vallee, B.L.: New human liver alcohol '
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'pubmed': 7011320},
22: {'info': 'Bosron, W.F.; Li, T.K.; Vallee, B.L.: New '
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'(1980) 77, 5784-5788.',
'pubmed': 7003596},
23: {'info': 'Bosron, W.F.; Li, T.K.; Dafeldecker, W.P.; '
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'dehydrogenase: kinetic and molecular properties. '
'Biochemistry (1979) 18, 1101-1105.',
'pubmed': 427099},
24: {'info': 'Dafeldecker, W.P.; Pares, X.; Vallee, B.L.; '
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'dehydrogenase: isolation and characterization of '
'isoenzymes from Saimiri sciureus. Biochemistry '
'(1981) 20, 856-861.',
'pubmed': 7011375},
25: {'info': 'Dafeldecker, W.P.; Meadow, P.E.; Pares, X.; '
'Vallee, B.L.: Simian liver alcohol dehydrogenase: '
'isolation and characterization of isoenzymes from '
'Macaca mulatta. Biochemistry (1981) 20, '
'6729-6734.',
'pubmed': 7030395},
26: {'info': 'Kvassman, J.; Pettersson, G.: Kinetics of '
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'in the pH range 10-12. Eur. J. Biochem. (1987) '
'166, 167-172.',
'pubmed': 3595610},
27: {'info': 'Andersson, L.; Mosbach, K.: Alcohol dehydrogenase '
'from horse liver by affinity chromatography. '
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295: {'info': 'Aquino Neto, S.; Forti, J.; Zucolotto, V.; '
'Ciancaglini, P.; de Andrade, A.: Development of '
'nanostructured bioanodes containing dendrimers '
'and dehydrogenases enzymes for application in '
'ethanol biofuel cells. Biosens. Bioelectron. '
'(2011) 26, 2922-2926.',
'pubmed': 21177091}}),
('tissues',
{'BTO:0000133',
'BTO:0000135',
'BTO:0000286',
'BTO:0000575',
'BTO:0000604',
'BTO:0000608',
'BTO:0000671',
'BTO:0000759',
'BTO:0000763',
'BTO:0000959',
'BTO:0000988',
'BTO:0001175',
'BTO:0001239',
'BTO:0001253',
'BTO:0001307',
'BTO:0001363',
'BTO:0001424',
'BTO:0001613'})])
© 2019-2022 Matthias König
نیازمندی
| مقدار | نام |
|---|---|
| >=0.1.7 | depinfo |
| >=0.2.10 | pymetadata |
| - | rich |
| - | requests |
| >=1.4.0 | pandas |
| >=3.0.9 | pyparsing |
| >=5.2.0 | ujson |
| >6.5.1 | pip-tools |
| >=22.1.0 | black |
| >=1.0.1 | bump2version |
| >=5.10.1 | isort |
| >=3.24.3 | tox |
| >=4.0.1 | flake8 |
| >=17.8.0 | flake8-mypy |
| >=0.931 | mypy |
| >=7.0.1 | pytest |
| >=3.0.0 | pytest-cov |
نحوه نصب
نصب پکیج whl brendapy-0.5.0:
pip install brendapy-0.5.0.whl
نصب پکیج tar.gz brendapy-0.5.0:
pip install brendapy-0.5.0.tar.gz