DB code: D00482

CATH domain 3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold
E.C. 1.1.1.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1 D00001 D00002 D00018 D00048 D00481 D00490 D00492 D00615

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P07327 Alcohol dehydrogenase 1A
EC 1.1.1.1
Alcohol dehydrogenase subunit alpha
NP_000658.1 (Protein)
NM_000667.3 (DNA/RNA sequence)
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]
P00325 Alcohol dehydrogenase 1B
EC 1.1.1.1
Alcohol dehydrogenase subunit beta
NP_000659.2 (Protein)
NM_000668.4 (DNA/RNA sequence)
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]
P40394 Alcohol dehydrogenase class 4 mu/sigma chain
EC 1.1.1.1
Alcohol dehydrogenase class IV mu/sigma chain
Retinol dehydrogenase
Gastric alcohol dehydrogenase
NP_000664.2 (Protein)
NM_000673.4 (DNA/RNA sequence)
NP_001159976.1 (Protein)
NM_001166504.1 (DNA/RNA sequence)
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]

KEGG enzyme name
alcohol dehydrogenase
aldehyde reductase
ADH
alcohol dehydrogenase (NAD)
aliphatic alcohol dehydrogenase
ethanol dehydrogenase
NAD-dependent alcohol dehydrogenase
NAD-specific aromatic alcohol dehydrogenase
NADH-alcohol dehydrogenase
NADH-aldehyde dehydrogenase
primary alcohol dehydrogenase
yeast alcohol dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P07327 ADH1A_HUMAN An alcohol + NAD(+) = an aldehyde or ketone + NADH. Dimer of identical or non-identical chains of three types, alpha, beta and gamma. Cytoplasm. Binds 2 zinc ions per subunit.
P00325 ADH1B_HUMAN An alcohol + NAD(+) = an aldehyde or ketone + NADH. Dimer of identical or non-identical chains of three types, alpha, beta and gamma. Cytoplasm. Binds 2 zinc ions per subunit.
P40394 ADH7_HUMAN An alcohol + NAD(+) = an aldehyde or ketone + NADH. Homodimer. Cytoplasm. Binds 2 zinc ions per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00071 Fatty acid metabolism
MAP00120 Bile acid biosynthesis
MAP00260 Glycine, serine and threonine metabolism
MAP00350 Tyrosine metabolism
MAP00624 1- and 2-Methylnaphthalene degradation
MAP00641 3-Chloroacrylic acid degradation
MAP00830 Retinol metabolism
MAP00980 Metabolism of xenobiotics by cytochrome P450
MAP00982 Drug metabolism - cytochrome P450

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00003 C00069 C00004 C00071 C00709 C00080
E.C.
Compound Zinc NAD+ Alcohol NADH Aldehyde Ketone H+
Type heavy metal amide group,amine group,nucleotide carbohydrate amide group,amine group,nucleotide carbohydrate carbohydrate others
ChEBI 29105
 29105
 		15846
 15846
 		16908
 16908
 		15378
 15378
PubChem 32051
 32051
 		5893
 5893
 		439153
 439153
 		1038
 1038
1hsoA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hsoB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1u3tA01 Bound:2x_ZN Unbound Unbound Unbound Bound:CCB Unbound
1u3tB01 Bound:2x_ZN Unbound Unbound Unbound Bound:CCB Unbound
1dehA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1dehB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hdxA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hdxB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hdyA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hdyB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hdzA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hdzB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hszA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1hszB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1htbA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1htbB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
3hudA01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
3hudB01 Bound:2x_ZN Unbound Unbound Unbound Unbound Unbound
1agnA01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_378
1agnB01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_378
1agnC01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_378
1agnD01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_378
1d1sA01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_501
1d1sB01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_506
1d1sC01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_505
1d1sD01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_511
1d1tA01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_501
1d1tB01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_506
1d1tC01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_505
1d1tD01 Bound:_ZN_376 Unbound Unbound Unbound Unbound Analogue:ACT_511
1hsoA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1hsoB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1u3tA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1u3tB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1dehA02 Unbound Analogue:NAD-PYZ Unbound Unbound Unbound Unbound
1dehB02 Unbound Analogue:NAD-PYZ Unbound Unbound Unbound Unbound
1hdxA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1hdxB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1hdyA02 Unbound Analogue:NAD-PYZ Unbound Unbound Unbound Unbound
1hdyB02 Unbound Analogue:NAD-PYZ Unbound Unbound Unbound Unbound
1hdzA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1hdzB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1hszA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1hszB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1htbA02 Unbound Analogue:NAD-PYZ Unbound Unbound Unbound Unbound
1htbB02 Unbound Analogue:NAD-PYZ Unbound Unbound Unbound Unbound
3hudA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
3hudB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1agnA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1agnB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1agnC02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1agnD02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1sA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1sB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1sC02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1sD02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1tA02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1tB02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1tC02 Unbound Bound:NAD Unbound Unbound Unbound Unbound
1d1tD02 Unbound Bound:NAD Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P40394, P00325, P00327, P00326, P00328,P26325

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1hsoA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hsoB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1u3tA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1u3tB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1dehA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1dehB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hdxA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hdxB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hdyA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hdyB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hdzA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding) mutant R47G
1hdzB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding) mutant R47G
1hszA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1hszB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1htbA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1htbB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
3hudA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
3hudB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1agnA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1agnB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1agnC01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1agnD01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1d1sA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1d1sB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1d1sC01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1d1sD01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
1d1tA01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding) mutant M141L
1d1tB01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding) mutant M141L
1d1tC01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding) mutant M141L
1d1tD01 THR 48;HIS 51 CYS 46;HIS 67;CYS 174(Catalytic zinc binding) mutant M141L
1hsoA02
1hsoB02
1u3tA02
1u3tB02
1dehA02
1dehB02
1hdxA02
1hdxB02
1hdyA02
1hdyB02
1hdzA02
1hdzB02
1hszA02
1hszB02
1htbA02
1htbB02
3hudA02
3hudB02
1agnA02
1agnB02
1agnC02
1agnD02
1d1sA02
1d1sB02
1d1sC02
1d1sD02
1d1tA02
1d1tB02
1d1tC02
1d1tD02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.4, p.1065-1067

References
[1]
Resource
Comments
Medline ID
PubMed ID 1772423
Journal Biochem Int
Year 1991
Volume 24
Pages 451-60
Authors Fong WP, Keung WM
Title Examination of subunit interaction in human ADH: carboxymethylation of the heterodimer beta 2 gamma 1.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1989677
Journal Biochemistry
Year 1991
Volume 30
Pages 1062-8
Authors Ehrig T, Hurley TD, Edenberg HJ, Bosron WF
Title General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 91376103
PubMed ID 1896463
Journal Proc Natl Acad Sci U S A
Year 1991
Volume 88
Pages 8149-53
Authors Hurley TD, Bosron WF, Hamilton JA, Amzel LM
Title Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.
Related PDB 3hud
Related UniProtKB P00325
[4]
Resource
Comments
Medline ID
PubMed ID 1572355
Journal Eur J Biochem
Year 1992
Volume 205
Pages 519-26
Authors Hoog JO, Eklund H, Jornvall H
Title A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme properties.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8493917
Journal Adv Exp Med Biol
Year 1993
Volume 328
Pages 391-400
Authors Plapp BV, Green DW, Sun HW, Park DH, Kim K
Title Substrate specificity of alcohol dehydrogenases.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8127901
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 1893-7
Authors Pares X, Cederlund E, Moreno A, Hjelmqvist L, Farres J, Jornvall H
Title Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin, and correlation with enzymology.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 7957193
Journal Eur J Biochem
Year 1994
Volume 225
Pages 1015-9
Authors Jelokova J, Karlsson C, Estonius M, Jornvall H, Hoog JO
Title Features of structural zinc in mammalian alcohol dehydrogenase. Site-directed mutagenesis of the zinc ligands.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
Medline ID 94260547
PubMed ID 8201622
Journal J Mol Biol
Year 1994
Volume 239
Pages 415-29
Authors Hurley TD, Bosron WF, Stone CL, Amzel LM
Title Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.
Related PDB 1hdx 1hdy 1hdz
Related UniProtKB P00325
[9]
Resource
Comments
Medline ID
PubMed ID 7484389
Journal Adv Exp Med Biol
Year 1995
Volume 372
Pages 281-94
Authors Jornvall H, Danielsson O, Hjelmqvist L, Persson B, Shafqat J
Title The alcohol dehydrogenase system.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7479907
Journal Proc Natl Acad Sci U S A
Year 1995
Volume 92
Pages 10904-8
Authors Hjelmqvist L, Estonius M, Jornvall H
Title The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of enzymogenesis.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8898073
Journal FEBS Lett
Year 1996
Volume 395
Pages 99-102
Authors Moreno A, Farres J, Pares X, Jornvall H, Persson B
Title Molecular modelling of human gastric alcohol dehydrogenase (class IV) and substrate docking: differences towards the classical liver enzyme (class I).
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 96291846
PubMed ID 8663387
Journal J Biol Chem
Year 1996
Volume 271
Pages 17057-61
Authors Davis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD
Title X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding.
Related PDB 1deh 1htb
Related UniProtKB P00325
[13]
Resource
Comments
Medline ID
PubMed ID 9059633
Journal Adv Exp Med Biol
Year 1997
Volume 414
Pages 291-302
Authors Hurley TD, Steinmetz CG, Xie P, Yang ZN
Title Three-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9059632
Journal Adv Exp Med Biol
Year 1997
Volume 414
Pages 281-9
Authors Jornvall H, Shafqat J, el-Ahmad M, Hjelmqvist L, Persson B, Danielsson O
Title Alcohol dehydrogenase variability. Evolutionary and functional conclusions from characterization of further variants.
Related PDB
Related UniProtKB
[15]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 97373546
PubMed ID 9228021
Journal J Biol Chem
Year 1997
Volume 272
Pages 18558-63
Authors Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD
Title X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity.
Related PDB 1agn
Related UniProtKB P40394
[16]
Resource
Comments
Medline ID
PubMed ID 9572895
Journal J Med Chem
Year 1998
Volume 41
Pages 1696-701
Authors Schindler JF, Berst KB, Plapp BV
Title Inhibition of human alcohol dehydrogenases by formamides.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 10352708
Journal Adv Exp Med Biol
Year 1999
Volume 463
Pages 373-7
Authors Persson B, Nordling E, Kallberg Y, Lundh D, Oppermann UC, Marschall HU, Jornvall H
Title Bioinformatics in studies of SDR and MDR enzymes.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10407146
Journal Biochim Biophys Acta
Year 1999
Volume 1432
Pages 239-50
Authors Foglio MH, Duester G
Title Molecular docking studies on interaction of diverse retinol structures with human alcohol dehydrogenases predict a broad role in retinoid ligand synthesis.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10631979
Journal Protein Sci
Year 1999
Volume 8
Pages 2639-44
Authors Xie PT, Hurley TD
Title Methionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase.
Related PDB 1d1s 1d1t
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 10829036
Journal J Biol Chem
Year 2000
Volume 275
Pages 25180-7
Authors Crosas B, Allali-Hassani A, Martinez SE, Martras S, Persson B, Jornvall H, Pares X, Farres J
Title Molecular basis for differential substrate specificity in class IV alcohol dehydrogenases: a conserved function in retinoid metabolism but not in ethanol oxidation.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 11306065
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 435-44
Authors Allali-Hassani A, Crosas B, Pares X, Farres J
Title Kinetic effects of a single-amino acid mutation in a highly variable loop (residues 114-120) of class IV ADH.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 11173978
Journal J Biomed Sci
Year 2001
Volume 8
Pages 71-6
Authors Hoog JO, Hedberg JJ, Stromberg P, Svensson S
Title Mammalian alcohol dehydrogenase - functional and structural implications.
Related PDB
Related UniProtKB
[23]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11274460
Journal Protein Sci
Year 2001
Volume 10
Pages 697-706
Authors Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD
Title Three-dimensional structures of the three human class I alcohol dehydrogenases.
Related PDB 1hso 1hsz 1ht0
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11942822
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 3858-64
Authors Kohen A, Jensen JH
Title Boundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 12604207
Journal Chem Biol Interact
Year 2003
Volume 143-144
Pages 219-27
Authors Yin SJ, Chou CF, Lai CL, Lee SL, Han CL
Title Human class IV alcohol dehydrogenase: kinetic mechanism, functional roles and medical relevance.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 14523561
Journal Cell Mol Life Sci
Year 2003
Volume 60
Pages 2009-16
Authors Hjelmqvist L, Norin A, El-Ahmad M, Griffiths W, Jornvall H
Title Distinct but parallel evolutionary patterns between alcohol and aldehyde dehydrogenases: addition of fish/human betaine aldehyde dehydrogenase divergence.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the human zinc-containing alcohol dehydrogenase class.
Although this enzyme binds two zinc ions, only one zinc is involved in catalysis. This enzyme catalyzes the similar reaction to that of its homologous enzyme (D00001 in EzCatDB). The hydride transfer reaction proceeds as follows:
(0) Catalytic zinc ion, which is bound to Cys46, His67 and Cys174 and the hydroxyl group of the substrate alcohol, may lower the pKa of the hydroxyl oxygen of the alcohol, facilitating its deprotonation.
(1) His51 may act as a general base to deprotonate the hydroxyl oxygen, through 2'-hydroxyl group of NAD+ ribose and Thr48 by a proton relay system, leading to an alkoxide transition-state.
(2) The hydrogen is transferred from the carbon atom of alcohol to the nicotinamide group in the NAD+. Thus, hydride transfer occurs.

Created Updated
2005-01-11 2010-09-09