DB code: S00227

CATH domain 3.20.20.100 : TIM Barrel Catalytic domain
E.C. 1.1.1.2
CSA 2alr
M-CSA 2alr
MACiE

CATH domain Related DB codes (homologues)
3.20.20.100 : TIM Barrel S00228 S00229

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P14550 Alcohol dehydrogenase {NADP+}
EC 1.1.1.2
Aldehyde reductase
Aldo-keto reductase family 1 member A1
NP_001189342.1 (Protein)
NM_001202413.1 (DNA/RNA sequence)
NP_001189343.1 (Protein)
NM_001202414.1 (DNA/RNA sequence)
NP_006057.1 (Protein)
NM_006066.3 (DNA/RNA sequence)
NP_697021.1 (Protein)
NM_153326.2 (DNA/RNA sequence)
PF00248 (Aldo_ket_red)
[Graphical View]

KEGG enzyme name
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+)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P14550 AK1A1_HUMAN An alcohol + NADP(+) = an aldehyde + NADPH. Monomer (By similarity).

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00561 Glycerolipid metabolism
MAP00930 Caprolactam degradation

Compound table
Substrates Products Intermediates
KEGG-id C00006 C00226 C00432 C00005 C00071
E.C.
Compound NADP+ Primary alcohol Secondary alcohol NADPH Aldehyde
Type amide group,amine group,nucleotide carbohydrate carbohydrate amide group,amine group,nucleotide carbohydrate
ChEBI 18009
18009
16474
16474
PubChem 5886
5886
5884
5884
2alrA Unbound Unbound Unbound Unbound Unbound
1hqtA Bound:NAP Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
see S00228

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2alrA ASP 44;TYR 49;LYS 79;HIS 112
1hqtA ASP 45; ;LYS 80;HIS 113 mutant Y50F

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.866-868
[3]
Fig.3

References
[1]
Resource
Comments
Medline ID
PubMed ID 3160340
Journal Biochem J
Year 1985
Volume 228
Pages 363-73
Authors Esterbauer H, Zollner H, Lang J
Title Metabolism of the lipid peroxidation product 4-hydroxynonenal by isolated hepatocytes and by liver cytosolic fractions.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS)
Medline ID
PubMed ID
Journal Acta Crystallogr D Biol Crystallogr
Year 1994
Volume 50
Pages 859-68
Authors El-Kabbani O, Green NC, Lin G, Carson M, Narayana SVL., Moore KM, Flynn TG, DeLucas LJ
Title Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications
Related PDB 2alr
Related UniProtKB P14550
[3]
Resource
Comments
Medline ID
PubMed ID 9521768
Journal Biochemistry
Year 1998
Volume 37
Pages 4482-9
Authors Cho H, Plapp BV
Title Specificity of alcohol dehydrogenases for sulfoxides.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10694410
Journal Biochemistry
Year 2000
Volume 39
Pages 2406-12
Authors Northrop DB, Cho YK
Title Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10651037
Journal Proteins
Year 2000
Volume 38
Pages 41-8
Authors Ye Q, Hyndman D, Li X, Flynn TG, Jia Z
Title Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily.
Related PDB 1c9w
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11279029
Journal J Biol Chem
Year 2001
Volume 276
Pages 19253-8
Authors Tryggvason K, Romert A, Eriksson U
Title Biosynthesis of 9-cis-retinoic acid in vivo. The roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11306083
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 651-8
Authors Ye Q, Hyndman D, Green NC, Li L, Jia Z, Flynn TG
Title The crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding.
Related PDB 1hqt
Related UniProtKB

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

Created Updated
2004-02-02 2009-09-28