EzCatDB: S00227

DB codeS00227
CATH domainDomain 13.20.20.100Catalytic domain
E.C.1.1.1.2
CSA2alr

CATH domainRelated DB codes (homologues)
3.20.20.100S00228,S00229

Enzyme Name
Swiss-protKEGG

P14550
Protein nameAlcohol dehydrogenase {NADP+}alcohol dehydrogenase (NADP+)
aldehyde reductase (NADPH2)
NADP-alcohol dehydrogenase
NADP+-aldehyde reductase
NADP+-dependent aldehyde reductase
NADPH-aldehyde reductase
NADPH-dependent aldehyde reductase
nonspecific succinic semialdehyde reductase
ALR 1
low-Km aldehyde reductase
high-Km aldehyde reductase
alcohol dehydrogenase (NADP+)
SynonymsEC 1.1.1.2
Aldehyde reductase
Aldo-keto reductase family 1 member A1

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00561Glycerolipid metabolism
MAP00930Caprolactam degradation

Swiss-prot:Accession NumberP14550
Entry nameAK1A1_HUMAN
ActivityAn alcohol + NADP(+) = an aldehyde + NADPH.
SubunitMonomer (By similarity).
Subcellular location
Cofactor


SubstratesProducts
KEGG-idC00006C00226C00432C00005C00071
CompoundNADP+Primary alcoholSecondary alcoholNADPHAldehyde
Typeamide group,amine group,nucleotidecarbohydratecarbohydrateamide group,amine group,nucleotidecarbohydrate
2alrAUnboundUnboundUnboundUnboundUnbound
1hqtABound:NAPUnboundUnboundUnboundUnbound

Active-site residues
resource
see S00228
pdbCatalytic residuescomment
2alrAASP 44;TYR 49;LYS 79;HIS 112

1hqtAASP 45;      ;LYS 80;HIS 113
mutant Y50F

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.866-868
[3]Fig.3

references
[1]
PubMed ID3160340
JournalBiochem J
Year1985
Volume228
Pages363-73
AuthorsEsterbauer H, Zollner H, Lang J
TitleMetabolism of the lipid peroxidation product 4-hydroxynonenal by isolated hepatocytes and by liver cytosolic fractions.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS)
JournalActa Crystallogr D Biol Crystallogr
Year1994
Volume50
Pages859-68
AuthorsEl-Kabbani O, Green NC, Lin G, Carson M, Narayana SVL., Moore KM, Flynn TG, DeLucas LJ
TitleStructures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications
Related PDB2alr
Related Swiss-protP14550
[3]
PubMed ID9521768
JournalBiochemistry
Year1998
Volume37
Pages4482-9
AuthorsCho H, Plapp BV
TitleSpecificity of alcohol dehydrogenases for sulfoxides.
[4]
PubMed ID10694410
JournalBiochemistry
Year2000
Volume39
Pages2406-12
AuthorsNorthrop DB, Cho YK
TitleEffect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis.
[5]
PubMed ID10651037
JournalProteins
Year2000
Volume38
Pages41-8
AuthorsYe Q, Hyndman D, Li X, Flynn TG, Jia Z
TitleCrystal structure of CHO reductase, a member of the aldo-keto reductase superfamily.
Related PDB1c9w
[6]
PubMed ID11279029
JournalJ Biol Chem
Year2001
Volume276
Pages19253-8
AuthorsTryggvason K, Romert A, Eriksson U
TitleBiosynthesis of 9-cis-retinoic acid in vivo. The roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases.
[7]
PubMed ID11306083
JournalChem Biol Interact
Year2001
Volume130-132
Pages651-8
AuthorsYe Q, Hyndman D, Green NC, Li L, Jia Z, Flynn TG
TitleThe crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding.
Related PDB1hqt

comments
This enzyme is homologous to aldose reductase (S00228 in EzCatDB), with the conserved catalytic residues.

createdupdated
2004-02-022009-09-28


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)

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