D00482
type: Enzyme
active site residues resources: P40394
active site residues resources: P00325
active site residues resources: P00327
active site residues resources: P00326
active site residues resources: P00328
cath: Quinone Oxidoreductase; Chain A, domain 1
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.1.1.1
kegg cofactor: Zinc
kegg enzyme: alcohol dehydrogenase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Fatty acid metabolism
kegg pathway: Bile acid biosynthesis
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Tyrosine metabolism
kegg pathway: 1- and 2-Methylnaphthalene degradation
kegg pathway: 3-Chloroacrylic acid degradation
kegg pathway: Retinol metabolism
kegg pathway: Metabolism of xenobiotics by cytochrome P450
kegg pathway: Drug metabolism - cytochrome P450
kegg product: NADH
kegg product: Aldehyde
kegg product: Ketone
kegg product: H+
kegg substrate: NAD+
kegg substrate: Alcohol
pdb: 1hsoA01
pdb: 1hsoB01
pdb: 1u3tA01
pdb: 1u3tB01
pdb: 1dehA01
pdb: 1dehB01
pdb: 1hdxA01
pdb: 1hdxB01
pdb: 1hdyA01
pdb: 1hdyB01
pdb: 1hdzA01
pdb: 1hdzB01
pdb: 1hszA01
pdb: 1hszB01
pdb: 1htbA01
pdb: 1htbB01
pdb: 3hudA01
pdb: 3hudB01
pdb: 1agnA01
pdb: 1agnB01
pdb: 1agnC01
pdb: 1agnD01
pdb: 1d1sA01
pdb: 1d1sB01
pdb: 1d1sC01
pdb: 1d1sD01
pdb: 1d1tA01
pdb: 1d1tB01
pdb: 1d1tC01
pdb: 1d1tD01
pdb: 1hsoA02
pdb: 1hsoB02
pdb: 1u3tA02
pdb: 1u3tB02
pdb: 1dehA02
pdb: 1dehB02
pdb: 1hdxA02
pdb: 1hdxB02
pdb: 1hdyA02
pdb: 1hdyB02
pdb: 1hdzA02
pdb: 1hdzB02
pdb: 1hszA02
pdb: 1hszB02
pdb: 1htbA02
pdb: 1htbB02
pdb: 3hudA02
pdb: 3hudB02
pdb: 1agnA02
pdb: 1agnB02
pdb: 1agnC02
pdb: 1agnD02
pdb: 1d1sA02

Analogue
compound: NAD+
ligand het code: NAD-PYZ
pdb: 1dehA02

Analogue
compound: NAD+
ligand het code: NAD-PYZ
pdb: 1dehB02

Analogue
compound: NAD+
ligand het code: NAD-PYZ
pdb: 1hdyA02

Analogue
compound: NAD+
ligand het code: NAD-PYZ
pdb: 1hdyB02

Analogue
compound: NAD+
ligand het code: NAD-PYZ
pdb: 1htbA02

Analogue
compound: NAD+
ligand het code: NAD-PYZ
pdb: 1htbB02

Analogue
compound: Ketone
ligand het code: ACT_378
pdb: 1agnA01

Analogue
compound: Ketone
ligand het code: ACT_378
pdb: 1agnB01

Analogue
compound: Ketone
ligand het code: ACT_378
pdb: 1agnC01

Analogue
compound: Ketone
ligand het code: ACT_378
pdb: 1agnD01

Analogue
compound: Ketone
ligand het code: ACT_501
pdb: 1d1sA01

Analogue
compound: Ketone
ligand het code: ACT_506
pdb: 1d1sB01

Analogue
compound: Ketone
ligand het code: ACT_505
pdb: 1d1sC01

Analogue
compound: Ketone
ligand het code: ACT_511
pdb: 1d1sD01

Analogue
compound: Ketone
ligand het code: ACT_501
pdb: 1d1tA01

Analogue
compound: Ketone
ligand het code: ACT_506
pdb: 1d1tB01

Analogue
compound: Ketone
ligand het code: ACT_505
pdb: 1d1tC01

Analogue
compound: Ketone
ligand het code: ACT_511
pdb: 1d1tD01

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.4, p.1065-1067

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720

Quinone Oxidoreductase; Chain A, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.90.180.10

H+
type: KeggProduct
compound type: others
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Fatty acid metabolism
type: KeggPathway
references: KEGG:MAP00071

Bile acid biosynthesis
type: KeggPathway
references: KEGG:MAP00120

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260

Tyrosine metabolism
type: KeggPathway
references: KEGG:MAP00350

1- and 2-Methylnaphthalene degradation
type: KeggPathway
references: KEGG:MAP00624

3-Chloroacrylic acid degradation
type: KeggPathway
references: KEGG:MAP00641

Retinol metabolism
type: KeggPathway
references: KEGG:MAP00830

Metabolism of xenobiotics by cytochrome P450
type: KeggPathway
references: KEGG:MAP00980

Drug metabolism - cytochrome P450
type: KeggPathway
references: KEGG:MAP00982

Examination of subunit interaction in human ADH: carboxymethylation of the heterodimer beta 2 gamma 1.
type: BibliographicResource
authors:
  item: Fong WP
  item: Keung WM
journal: Biochem Int
pages: 451-60
published year: 1991
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/1772423

The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of enzymogenesis.
type: BibliographicResource
authors:
  item: Hjelmqvist L
  item: Estonius M
  item: Jornvall H
journal: Proc Natl Acad Sci U S A
pages: 10904-8
published year: 1995
volume: 92
references: http://www.ncbi.nlm.nih.gov/pubmed/7479907

Molecular modelling of human gastric alcohol dehydrogenase (class IV) and substrate docking: differences towards the classical liver enzyme (class I).
type: BibliographicResource
authors:
  item: Moreno A
  item: Farres J
  item: Pares X
  item: Jornvall H
  item: Persson B
journal: FEBS Lett
pages: 99-102
published year: 1996
volume: 395
references: http://www.ncbi.nlm.nih.gov/pubmed/8898073

X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding.
type: BibliographicResource
authors:
  item: Davis GJ
  item: Bosron WF
  item: Stone CL
  item: Owusu-Dekyi K
  item: Hurley TD
journal: J Biol Chem
medline id: 96291846
pages: 17057-61
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8663387
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00325
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Three-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity.
type: BibliographicResource
authors:
  item: Hurley TD
  item: Steinmetz CG
  item: Xie P
  item: Yang ZN
journal: Adv Exp Med Biol
pages: 291-302
published year: 1997
volume: 414
references: http://www.ncbi.nlm.nih.gov/pubmed/9059633

Alcohol dehydrogenase variability. Evolutionary and functional conclusions from characterization of further variants.
type: BibliographicResource
authors:
  item: Jornvall H
  item: Shafqat J
  item: el-Ahmad M
  item: Hjelmqvist L
  item: Persson B
  item: Danielsson O
journal: Adv Exp Med Biol
pages: 281-9
published year: 1997
volume: 414
references: http://www.ncbi.nlm.nih.gov/pubmed/9059632

X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity.
type: BibliographicResource
authors:
  item: Xie P
  item: Parsons SH
  item: Speckhard DC
  item: Bosron WF
  item: Hurley TD
journal: J Biol Chem
medline id: 97373546
pages: 18558-63
published year: 1997
volume: 272
references: http://www.ncbi.nlm.nih.gov/pubmed/9228021
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P40394
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Inhibition of human alcohol dehydrogenases by formamides.
type: BibliographicResource
authors:
  item: Schindler JF
  item: Berst KB
  item: Plapp BV
journal: J Med Chem
pages: 1696-701
published year: 1998
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/9572895

Bioinformatics in studies of SDR and MDR enzymes.
type: BibliographicResource
authors:
  item: Persson B
  item: Nordling E
  item: Kallberg Y
  item: Lundh D
  item: Oppermann UC
  item: Marschall HU
  item: Jornvall H
journal: Adv Exp Med Biol
pages: 373-7
published year: 1999
volume: 463
references: http://www.ncbi.nlm.nih.gov/pubmed/10352708

Molecular docking studies on interaction of diverse retinol structures with human alcohol dehydrogenases predict a broad role in retinoid ligand synthesis.
type: BibliographicResource
authors:
  item: Foglio MH
  item: Duester G
journal: Biochim Biophys Acta
pages: 239-50
published year: 1999
volume: 1432
references: http://www.ncbi.nlm.nih.gov/pubmed/10407146

Methionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase.
type: BibliographicResource
authors:
  item: Xie PT
  item: Hurley TD
journal: Protein Sci
pages: 2639-44
published year: 1999
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10631979
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase.
type: BibliographicResource
authors:
  item: Ehrig T
  item: Hurley TD
  item: Edenberg HJ
  item: Bosron WF
journal: Biochemistry
pages: 1062-8
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1989677

Molecular basis for differential substrate specificity in class IV alcohol dehydrogenases: a conserved function in retinoid metabolism but not in ethanol oxidation.
type: BibliographicResource
authors:
  item: Crosas B
  item: Allali-Hassani A
  item: Martinez SE
  item: Martras S
  item: Persson B
  item: Jornvall H
  item: Pares X
  item: Farres J
journal: J Biol Chem
pages: 25180-7
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/10829036

Kinetic effects of a single-amino acid mutation in a highly variable loop (residues 114-120) of class IV ADH.
type: BibliographicResource
authors:
  item: Allali-Hassani A
  item: Crosas B
  item: Pares X
  item: Farres J
journal: Chem Biol Interact
pages: 435-44
published year: 2001
volume: 130-132
references: http://www.ncbi.nlm.nih.gov/pubmed/11306065

Mammalian alcohol dehydrogenase - functional and structural implications.
type: BibliographicResource
authors:
  item: Hoog JO
  item: Hedberg JJ
  item: Stromberg P
  item: Svensson S
journal: J Biomed Sci
pages: 71-6
published year: 2001
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/11173978

Three-dimensional structures of the three human class I alcohol dehydrogenases.
type: BibliographicResource
authors:
  item: Niederhut MS
  item: Gibbons BJ
  item: Perez-Miller S
  item: Hurley TD
journal: Protein Sci
pages: 697-706
published year: 2001
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/11274460
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Boundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling.
type: BibliographicResource
authors:
  item: Kohen A
  item: Jensen JH
journal: J Am Chem Soc
pages: 3858-64
published year: 2002
volume: 124
references: http://www.ncbi.nlm.nih.gov/pubmed/11942822

Human class IV alcohol dehydrogenase: kinetic mechanism, functional roles and medical relevance.
type: BibliographicResource
authors:
  item: Yin SJ
  item: Chou CF
  item: Lai CL
  item: Lee SL
  item: Han CL
journal: Chem Biol Interact
pages: 219-27
published year: 2003
volume: 143-144
references: http://www.ncbi.nlm.nih.gov/pubmed/12604207

Distinct but parallel evolutionary patterns between alcohol and aldehyde dehydrogenases: addition of fish/human betaine aldehyde dehydrogenase divergence.
type: BibliographicResource
authors:
  item: Hjelmqvist L
  item: Norin A
  item: El-Ahmad M
  item: Griffiths W
  item: Jornvall H
journal: Cell Mol Life Sci
pages: 2009-16
published year: 2003
volume: 60
references: http://www.ncbi.nlm.nih.gov/pubmed/14523561

Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.
type: BibliographicResource
authors:
  item: Hurley TD
  item: Bosron WF
  item: Hamilton JA
  item: Amzel LM
journal: Proc Natl Acad Sci U S A
medline id: 91376103
pages: 8149-53
published year: 1991
volume: 88
references: http://www.ncbi.nlm.nih.gov/pubmed/1896463
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00325
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme properties.
type: BibliographicResource
authors:
  item: Hoog JO
  item: Eklund H
  item: Jornvall H
journal: Eur J Biochem
pages: 519-26
published year: 1992
volume: 205
references: http://www.ncbi.nlm.nih.gov/pubmed/1572355

Substrate specificity of alcohol dehydrogenases.
type: BibliographicResource
authors:
  item: Plapp BV
  item: Green DW
  item: Sun HW
  item: Park DH
  item: Kim K
journal: Adv Exp Med Biol
pages: 391-400
published year: 1993
volume: 328
references: http://www.ncbi.nlm.nih.gov/pubmed/8493917

Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin, and correlation with enzymology.
type: BibliographicResource
authors:
  item: Pares X
  item: Cederlund E
  item: Moreno A
  item: Hjelmqvist L
  item: Farres J
  item: Jornvall H
journal: Proc Natl Acad Sci U S A
pages: 1893-7
published year: 1994
volume: 91
references: http://www.ncbi.nlm.nih.gov/pubmed/8127901

Features of structural zinc in mammalian alcohol dehydrogenase. Site-directed mutagenesis of the zinc ligands.
type: BibliographicResource
authors:
  item: Jelokova J
  item: Karlsson C
  item: Estonius M
  item: Jornvall H
  item: Hoog JO
journal: Eur J Biochem
pages: 1015-9
published year: 1994
volume: 225
references: http://www.ncbi.nlm.nih.gov/pubmed/7957193

Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.
type: BibliographicResource
authors:
  item: Hurley TD
  item: Bosron WF
  item: Stone CL
  item: Amzel LM
journal: J Mol Biol
medline id: 94260547
pages: 415-29
published year: 1994
volume: 239
references: http://www.ncbi.nlm.nih.gov/pubmed/8201622
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00325
comment: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).

The alcohol dehydrogenase system.
type: BibliographicResource
authors:
  item: Jornvall H
  item: Danielsson O
  item: Hjelmqvist L
  item: Persson B
  item: Shafqat J
journal: Adv Exp Med Biol
pages: 281-94
published year: 1995
volume: 372
references: http://www.ncbi.nlm.nih.gov/pubmed/7484389

1u3tA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1u3t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u3t

1u3tB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1u3t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u3t

1agnA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1agn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1agn

1agnB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1agn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1agn

1agnC01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1agn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1agn

1agnD01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1agn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1agn

1d1sA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1s

1d1sB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1s

1d1sC01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1s

1d1sD01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1s

1d1tA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1t
comment: mutant M141L

1d1tB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1t
comment: mutant M141L

1d1tC01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1t
comment: mutant M141L

1d1tD01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1d1t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d1t
comment: mutant M141L

1dehA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1deh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1deh

1dehB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1deh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1deh

1hdxA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hdx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hdx

1hdxB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hdx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hdx

1hdyA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hdy

1hdyB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hdy

1hdzA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hdz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hdz
comment: mutant R47G

1hdzB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hdz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hdz
comment: mutant R47G

1hsoA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hso

1hsoB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hso

1hszA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hsz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hsz

1hszB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1hsz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hsz

1htbA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1htb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htb

1htbB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 1htb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htb

3hudA01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 3hud
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hud

3hudB01
type: Pdb
catalytic residue: THR 48;HIS 51
cofactor binding residue: CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
references: 3hud
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hud

Zinc
type: KeggCofactor
compound type: heavy metal
references: KEGG:C00038
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggSubstrate
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00003
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Aldehyde
type: KeggProduct
compound type: carbohydrate
references: KEGG:C00071

NADH
type: KeggProduct
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00004
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Alcohol
type: KeggSubstrate
compound type: carbohydrate
references: KEGG:C00069

Ketone
type: KeggProduct
compound type: carbohydrate
references: KEGG:C00709

aldehyde reductase
type: KeggEnzyme

ADH
type: KeggEnzyme

alcohol dehydrogenase (NAD)
type: KeggEnzyme

aliphatic alcohol dehydrogenase
type: KeggEnzyme

ethanol dehydrogenase
type: KeggEnzyme

NAD-dependent alcohol dehydrogenase
type: KeggEnzyme

NAD-specific aromatic alcohol dehydrogenase
type: KeggEnzyme

NADH-alcohol dehydrogenase
type: KeggEnzyme

NADH-aldehyde dehydrogenase
type: KeggEnzyme

primary alcohol dehydrogenase
type: KeggEnzyme

yeast alcohol dehydrogenase
type: KeggEnzyme