EC 1.1.1.2 - Alcohol dehydrogenase (NADP+)

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.1.1.2

Names

Accepted name:
alcohol dehydrogenase (NADP+)
Other names:
ALR 1
NADP+-alcohol dehydrogenase
NADP+-aldehyde reductase
NADP+-dependent aldehyde reductase
NADPH-aldehyde reductase
NADPH-dependent aldehyde reductase
aldehyde reductase (NADPH)
high-Km aldehyde reductase
low-Km aldehyde reductase
nonspecific succinic semialdehyde reductase
Systematic name:
alcohol:NADP+ oxidoreductase

Reaction

Cofactor

Comments:

A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00061
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008106
CAS Registry Number: 9028-12-0
UniProtKB/Swiss-Prot: (26) [show] [UniProt]

References

  1. Bosron, W.F. and Prairie, R.L.
    Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex.
    J. Biol. Chem. 247: 4480-4485 (1972). [PMID: 4402936]
  2. DeMoss, R.
    Triphosphopyridine nucleotide-specific ethanol dehydrogenase from Leuconostoc mesenteroides.
    Bacteriol. Proc. 81 (1953).
  3. Reeves, R.E., Montalvo, F.E. and Lushbaugh, T.S.
    Nicotinamide-adenine dinucleotide phosphate-dependent alcohol dehydrogenase. Enzyme from Entamoeba histolytica and some enzyme inhibitors.
    Int. J. Biochem. 2: 55-64 (1971).
  4. Tabakoff, B. and Erwin, V.G.
    Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain.
    J. Biol. Chem. 245: 3263-3268 (1970). [PMID: 4393513]

[EC 1.1.1.2 created 1961]