|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Marked as unbalanced.
Enzyme Commission Primary Name: alcohol dehydrogenase (NADP+)
Enzyme Commission Synonyms: 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)
Enzyme Commission Summary:
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 184.108.40.206, glucuronate reductase, EC 220.127.116.11, mevaldate reductase (NADPH) and EC 18.104.22.168, lactaldehyde reductase (NADPH). Re-specific with respect to NADPH.
Instance reaction of [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (22.214.171.124):
i3: acetaldehyde + NADP+ + H2O → acetate + NADPH + 2 H+ (126.96.36.199)
Instance reactions of [an alcohol + NADP+ = an aldehyde + NADPH + H+] (188.8.131.52):
i1: (S)-propane-1,2-diol + NADP+ = (S)-lactaldehyde + NADPH + H+ (1.1.1.-)
i2: (R)-propane-1,2-diol + NADP+ = (R)-lactaldehyde + NADPH + H+ (1.1.1.-)
Bosron72: Bosron WF, Prairie RL (1972). "Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex." J Biol Chem 247(14);4480-5. PMID: 4402936
Chen03c: Chen CN, Porubleva L, Shearer G, Svrakic M, Holden LG, Dover JL, Johnston M, Chitnis PR, Kohl DH (2003). "Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae." Yeast 20(6);545-54. PMID: 12722185
Murata85: Murata K, Fukuda Y, Simosaka M, Watanabe K, Saikusa T, Kimura A (1985). "Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae." Eur J Biochem 151(3);631-6. PMID: 3896793
Tabakoff70: Tabakoff B, Erwin VG (1970). "Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain." J Biol Chem 245(12);3263-8. PMID: 4393513
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493