DB code: D00481

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 D00482 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 D00482 D00490 D00492 D00615

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q9QYY9 Alcohol dehydrogenase 4
EC 1.1.1.1
Alcohol dehydrogenase class II
Alcohol dehydrogenase II
ADH2
NP_036126.2 (Protein)
NM_011996.2 (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
Q9QYY9 ADH4_MOUSE An alcohol + NAD(+) = an aldehyde or ketone + NADH. Dimer. Cytoplasm (By similarity). 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 C00071 C00709 C00004 C00080
E.C.
Compound Zinc NAD+ Alcohol Aldehyde Ketone NADH H+
Type heavy metal amide group,amine group,nucleotide carbohydrate carbohydrate carbohydrate amide group,amine group,nucleotide others
ChEBI 29105
 29105
 		15846
 15846
 		16908
 16908
 		15378
 15378
PubChem 32051
 32051
 		5893
 5893
 		439153
 439153
 		1038
 1038
1e3eA01 Bound:_ZN_378 Unbound Unbound Unbound Unbound Unbound
1e3eB01 Bound:_ZN_378 Unbound Unbound Unbound Unbound Unbound
1e3iA01 Bound:_ZN_380 Unbound Unbound Analogue:CXF Unbound Unbound
1e3iB01 Bound:_ZN_380 Unbound Unbound Analogue:CXF Unbound Unbound
1e3lA01 Bound:_ZN_380 Unbound Unbound Unbound Unbound Unbound
1e3lB01 Bound:_ZN_380 Unbound Unbound Unbound Unbound Unbound
1e3eA02 Unbound Unbound Unbound Unbound Unbound Bound:NAD
1e3eB02 Unbound Unbound Unbound Unbound Unbound Bound:NAD
1e3iA02 Unbound Unbound Unbound Unbound Unbound Bound:NAD
1e3iB02 Unbound Unbound Unbound Unbound Unbound Bound:NAD
1e3lA02 Unbound Unbound Unbound Unbound Unbound Bound:NAD
1e3lB02 Unbound Unbound Unbound Unbound Unbound Bound:NAD

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
1e3eA01 THR 48 CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
1e3eB01 THR 48 CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
1e3iA01 THR 48 CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
1e3iB01 THR 48 CYS 46;HIS 67;CYS 178(Catalytic Zinc binding)
1e3lA01 THR 48 CYS 46;HIS 67;CYS 178(Catalytic Zinc binding) mutant P47H
1e3lB01 THR 48 CYS 46;HIS 67;CYS 178(Catalytic Zinc binding) mutant P47H
1e3eA02
1e3eB02
1e3iA02
1e3iB02
1e3lA02
1e3lB02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[7]
p.450-451
[8]
p.346-348
[11]
Figure 3 p.3859

References
[1]
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
[2]
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
[3]
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
[4]
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
[5]
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
[6]
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
[7]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10970744
Journal J Mol Biol
Year 2000
Volume 302
Pages 441-53
Authors Svensson S, Hoog JO, Schneider G, Sandalova T
Title Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency.
Related PDB 1e3e 1e3i 1e3l
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11306056
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 339-50
Authors Svensson S, Stromberg P, Sandalova T, Hoog J
Title Class II alcohol dehydrogenase (ADH2)--adding the structure.
Related PDB
Related UniProtKB
[9]
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
[10]
Resource
Comments
Medline ID
PubMed ID 11964133
Journal Cell Mol Life Sci
Year 2002
Volume 59
Pages 552-9
Authors Stromberg P, Svensson S, Hedberg JJ, Nordling E, Hoog JO
Title Identification and characterisation of two allelic forms of human alcohol dehydrogenase 2.
Related PDB
Related UniProtKB
[11]
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

Comments
This enzyme belongs to the zinc-containing alcohol dehydrogenase class II.
According to the literature [7] & [8], this enzyme is inefficient, probably due to Pro47, whose mutation to His restores the activity.

Created Updated
2005-01-11 2009-02-26