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Escherichia coli K-12 substr. MG1655 Reaction: 1.1.1.2


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.1.1.2

Enzymes and Genes:
NADP+-dependent aldehyde reductaseInferred from experiment: ybbO
aldehyde reductase, NADPH-dependentInferred from experiment: ahr
aldehyde reductase, NADPH-dependentInferred from experiment: yahK
NADPH-dependent aldehyde reductaseInferred from experiment: yqhD

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Marked as unbalanced.

Instance reactions:
(R)-lactaldehyde + NADPH + H+ → (R)-propane-1,2-diol + NADP+ (1.1.1.-)

(S)-lactaldehyde + NADPH + H+ → (S)-propane-1,2-diol + NADP+ (1.1.1.-)

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 1.1.1.19, 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.

Citations: [Bosron72, Tabakoff70, Murata85, Chen03b]

Gene-Reaction Schematic

Expand/Contract the Schematic connections:

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:1.1.1.2, ENZYME:EC:1.1.1.2, IUBMB-ExplorEnz:EC:1.1.1.2


References

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

Chen03b: 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


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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