| EC |
1.1.1.2 |
| Accepted name: |
alcohol dehydrogenase (NADP+) |
| Reaction: |
an alcohol + NADP+ = an aldehyde + NADPH + H+ |
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For diagram of mevalonate biosynthesis, click here |
| Other name(s): |
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) |
| Systematic name: |
alcohol:NADP+ oxidoreductase |
| 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) and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH. |
| Links to other databases: |
BRENDA, EXPASY, GENE, KEGG, MetaCyc, PDB, CAS registry number: 9028-12-0 |
| 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 (1972) 4480–4485. [PMID: 4402936] |
| 2. |
DeMoss, R. Triphosphopyridine nucleotide-specific ethanol dehydrogenase from Leuconostoc mesenteroides. Bacteriol. Proc. (1953) 81. |
| 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 (1971) 55–64. |
| 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 (1970) 3263–3268. [PMID: 4393513] |
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| [EC 1.1.1.2 created 1961] |
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