EzCatDB: D00018

DB codeD00018
CATH domainDomain 13.90.180.10Catalytic domain
Domain 23.40.50.720Catalytic domain
E.C.1.1.1.1,1.1.1.284,1.1.1.-
CSA1teh

CATH domainRelated DB codes (homologues)
3.40.50.720S00543,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,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,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
3.90.180.10D00001,D00002,D00048,D00481,D00482,D00490,D00492,D00615

Enzyme Name
Swiss-protKEGG

P11766
Protein nameAlcohol dehydrogenase class-3alcohol dehydrogenase
   (EC 1.1.1.1)

aldehyde reductase
   (EC 1.1.1.1)

ADH
   (EC 1.1.1.1)

alcohol dehydrogenase (NAD)
   (EC 1.1.1.1)

aliphatic alcohol dehydrogenase
   (EC 1.1.1.1)

ethanol dehydrogenase
   (EC 1.1.1.1)

NAD-dependent alcohol dehydrogenase
   (EC 1.1.1.1)

NAD-specific aromatic alcohol dehydrogenase
   (EC 1.1.1.1)

NADH-alcohol dehydrogenase
   (EC 1.1.1.1)

NADH-aldehyde dehydrogenase
   (EC 1.1.1.1)

primary alcohol dehydrogenase
   (EC 1.1.1.1)

yeast alcohol dehydrogenase
   (EC 1.1.1.1)

S-(hydroxymethyl)glutathione dehydrogenase
   (EC 1.1.1.284)

NAD-linked formaldehyde dehydrogenase (incorrect)
   (EC 1.1.1.284)

formaldehyde dehydrogenase (incorrect)
   (EC 1.1.1.284)

formic dehydrogenase (incorrect)
   (EC 1.1.1.284)

class III alcohol dehydrogenase
   (EC 1.1.1.284)

ADH3
   (EC 1.1.1.284)

&chi
   (EC 1.1.1.284)

-ADH
   (EC 1.1.1.284)

FDH (incorrect)
   (EC 1.1.1.284)

formaldehyde dehydrogenase (glutathione) (incorrect)
   (EC 1.1.1.284)

GS-FDH (incorrect)
   (EC 1.1.1.284)

glutathione-dependent formaldehyde dehydrogenase (incorrect)
   (EC 1.1.1.284)

NAD-dependent formaldehyde dehydrogenase
   (EC 1.1.1.284)

GD-FALDH
   (EC 1.1.1.284)

NAD- and glutathione-dependent formaldehyde dehydrogenase
   (EC 1.1.1.284)

SynonymsEC 1.1.1.1
Alcohol dehydrogenase class-III
Alcohol dehydrogenase 5
Alcohol dehydrogenase class chi chain
S-(hydroxymethyl)glutathione dehydrogenase
EC 1.1.1.284
Glutathione-dependent formaldehyde dehydrogenase
GSH-FDH
FALDH
FDH
EC 1.1.1.-

KEGG pathways
MAP codePathwaysE.C.
MAP00010Glycolysis / Gluconeogenesis1.1.1.1
MAP00071Fatty acid metabolism1.1.1.1
MAP00120Bile acid biosynthesis1.1.1.1
MAP00260Glycine, serine and threonine metabolism1.1.1.1
MAP00350Tyrosine metabolism1.1.1.1
MAP006241- and 2-Methylnaphthalene degradation1.1.1.1
MAP006413-Chloroacrylic acid degradation1.1.1.1
MAP00680Methane metabolism1.1.1.284
MAP00830Retinol metabolism1.1.1.1
MAP00980Metabolism of xenobiotics by cytochrome P4501.1.1.1
MAP00982Drug metabolism - cytochrome P4501.1.1.1

Swiss-prot:Accession NumberP11766
Entry nameADHX_HUMAN
ActivityAn alcohol + NAD(+) = an aldehyde or ketone + NADH.,S-(hydroxymethyl)glutathione + NAD(P)(+) = S- formylglutathione + NAD(P)H.
SubunitHomodimer.
Subcellular locationCytoplasm.
CofactorBinds 2 zinc ions per subunit.


CofactorsSubstratesProducts
KEGG-idC00038C00003C00069C14180C00004C00071C00709C01031C00080
E.C.
1.1.1.1,1.1.1.2841.1.1.11.1.1.2841.1.1.1,1.1.1.2841.1.1.11.1.1.11.1.1.2841.1.1.1,1.1.1.284
CompoundZincNAD+AlcoholS-(Hydroxymethyl)glutathioneNADHAldehydeKetoneS-FormylglutathioneH+
Typeheavy metalamide group,amine group,nucleotidecarbohydrateamino acids,carbohydrate,carboxyl group,peptide/protein,sulfide groupamide group,amine group,nucleotidecarbohydratecarbohydrateamino acids,carbohydrate,carboxyl group,peptide/protein,sulfide groupothers
1m6hA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1m6hB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1m6wA01Bound:2x_ZNUnboundBound:12HUnboundUnboundUnboundUnboundUnbound
1m6wB01Bound:2x_ZNUnboundBound:12HUnboundUnboundUnboundUnboundUnbound
1ma0A01Bound:2x_ZNUnboundAnalogue:DAOUnboundUnboundUnboundUnboundUnbound
1ma0B01Bound:2x_ZNUnboundAnalogue:DAOUnboundUnboundUnboundUnboundUnbound
1mc5A01Bound:2x_ZNUnboundUnboundBound:AHEUnboundUnboundUnboundUnbound
1mc5B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1mp0A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1mp0B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tehA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1tehB01Bound:3x_ZNUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1m6hA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1m6hB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1m6wA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1m6wB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ma0A02UnboundBound:NADUnboundUnboundUnboundUnboundUnboundUnbound
1ma0B02UnboundBound:NADUnboundUnboundUnboundUnboundUnboundUnbound
1mc5A02UnboundUnboundUnboundUnboundBound:NADUnboundUnboundUnbound
1mc5B02UnboundUnboundUnboundUnboundBound:NADUnboundUnboundUnbound
1mp0A02UnboundUnboundUnboundUnboundBound:NADUnboundUnboundUnbound
1mp0B02UnboundUnboundUnboundUnboundBound:NADUnboundUnboundUnbound
1tehA02UnboundBound:NADUnboundUnboundUnboundUnboundUnboundUnbound
1tehB02UnboundBound:NADUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1teh & Swiss-prot;P11766 & literature [10]
pdbCatalytic residuesCofactor-binding residues
1m6hA01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1m6hB01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1m6wA01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1m6wB01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1ma0A01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1ma0B01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1mc5A01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1mc5B01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1mp0A01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1mp0B01THR 46
CYS  44;HIS  66;GLU  67;CYS 173(Catalytic zinc binding);CYS  96;CYS  99;CYS 102;CYS 110(Zinc binding)
1tehA01THR 48
CYS  46;HIS  67;GLU  68;CYS 174(Catalytic zinc binding);CYS  97;CYS 100;CYS 103;CYS 111(Zinc binding)
1tehB01THR 48
CYS  46;HIS  67;GLU  68;CYS 174(Catalytic zinc binding);CYS  97;CYS 100;CYS 103;CYS 111(Zinc binding)
1m6hA02

1m6hB02

1m6wA02

1m6wB02

1ma0A02

1ma0B02

1mc5A02

1mc5B02

1mp0A02

1mp0B02

1tehA02

1tehB02


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]p.337-340
[11]p.15194
[12]


references
[1]
PubMed ID6385855
JournalArch Biochem Biophys
Year1984
Volume233
Pages447-56
AuthorsLangston-Unkefer PJ, Gander JE
TitleOccurrence of multiple forms of alcohol dehydrogenase in Penicillium supplemented with 2,3-butanediol.
[2]
PubMed ID2688201
JournalTrends Biochem Sci
Year1989
Volume14
Pages368-73
AuthorsKlinman JP
TitleQuantum mechanical effects in enzyme-catalysed hydrogen transfer reactions.
[3]
PubMed ID1985938
JournalJ Biol Chem
Year1991
Volume266
Pages1128-33
AuthorsMoreno A, Pares X
TitlePurification and characterization of a new alcohol dehydrogenase from human stomach.
[4]
PubMed ID8493900
JournalAdv Exp Med Biol
Year1993
Volume328
Pages245-50
AuthorsHurley TD, Yang Z, Bosron WF, Weiner H
TitleCrystallization and preliminary X-ray analysis of bovine mitochondrial aldehyde dehydrogenase and human glutathione-dependent formaldehyde dehydrogenase.
[5]
CommentsMUTAGENESIS OF ARG-114
Medline ID93211987
PubMed ID8460164
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages2491-4
AuthorsEngeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL
TitleMutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation.
Related Swiss-protP11766
[6]
PubMed ID7957198
JournalEur J Biochem
Year1994
Volume225
Pages1081-8
AuthorsDanielsson O, Shafqat J, Estonius M, Jornvall H
TitleAlcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization.
[7]
PubMed ID8931553
JournalBiochemistry
Year1996
Volume35
Pages14561-8
AuthorsDanielsson O, Shafqat J, Estonius M, el-Ahmad M, Jornvall H
TitleIsozyme multiplicity with anomalous dimer patterns in a class III alcohol dehydrogenase. Effects on the activity and quaternary structure of residue exchanges at "nonfunctional" sites in a native protein.
[8]
PubMed ID8944774
JournalEur J Biochem
Year1996
Volume241
Pages849-57
AuthorsMartinez MC, Achkor H, Persson B, Fernandez MR, Shafqat J, Farres J, Jornvall H, Pares X
TitleArabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class p and liver class I alcohol dehydrogenases.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID97170743
PubMed ID9018047
JournalJ Mol Biol
Year1997
Volume265
Pages330-43
AuthorsYang ZN, Bosron WF, Hurley TD
TitleStructure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase.
Related PDB1teh
Related Swiss-protP11766
[10]
PubMed ID9613842
JournalProtein Eng
Year1998
Volume11
Pages185-98
AuthorsJongejan A, Jongejan JA, Duine JA
TitleHomology model of the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni.
[11]
CommentsX-ray crystallography
PubMed ID12484756
JournalBiochemistry
Year2002
Volume41
Pages15189-94
AuthorsSanghani PC, Bosron WF, Hurley TD
TitleHuman glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation.
Related PDB1mc5
[12]
CommentsX-ray crystallography
PubMed ID12196016
JournalBiochemistry
Year2002
Volume41
Pages10778-86
AuthorsSanghani PC, Robinson H, Bosron WF, Hurley TD
TitleHuman glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes.
Related PDB1m6h,1m6w,1ma0
[13]
PubMed ID14523561
JournalCell Mol Life Sci
Year2003
Volume60
Pages2009-16
AuthorsHjelmqvist L, Norin A, El-Ahmad M, Griffiths W, Jornvall H
TitleDistinct but parallel evolutionary patterns between alcohol and aldehyde dehydrogenases: addition of fish/human betaine aldehyde dehydrogenase divergence.
[14]
CommentsX-ray crystallography
PubMed ID12604204
JournalChem Biol Interact
Year2003
Volume143-144
Pages195-200
AuthorsSanghani PC, Robinson H, Bennett-Lovsey R, Hurley TD, Bosron WF
TitleStructure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase).
Related PDB1mp0
[15]
PubMed ID14960302
JournalFEBS Lett
Year2004
Volume559
Pages27-32
AuthorsNorin A, Shafqat J, El-Ahmad M, Alvelius G, Cederlund E, Hjelmqvist L, Jornvall H
TitleClass III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme.

comments
The E.C. was transferred from 1.2.1.1 to 1.1.1.284.
There are several isozymes of alcohol dehydrogenase in human; class-I, class-II, class-III, class-IV, & class-V. This enzyme belongs to the class-III isozyme.

createdupdated
2004-03-242009-03-16


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.