Aldehyde dehydrogenase (NAD+)

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aldehyde dehydrogenase (NAD)
1cw3.jpg
Aldehyde dehydrogenase tetramer, Human
Identifiers
EC number1.2.1.3
CAS number9028-86-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, an aldehyde dehydrogenase (NAD+) (EC 1.2.1.3) is an enzyme that catalyzes the chemical reaction

an aldehyde + NAD+ + H2O an acid + NADH + H+

The 3 substrates of this enzyme are aldehyde, NAD+, and H2O, whereas its 3 products are acid, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aldehyde:NAD+ oxidoreductase. Other names in common use include CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, NAD-aldehyde dehydrogenase, NAD-dependent 4-hydroxynonenal dehydrogenase, NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, propionaldehyde dehydrogenase, and aldehyde dehydrogenase (NAD). This enzyme participates in 17 metabolic pathways: glycolysis / gluconeogenesis, ascorbate and aldarate metabolism, fatty acid metabolism, bile acid biosynthesis, urea cycle and metabolism of amino groups, valine, leucine and isoleucine degradation, lysine degradation, histidine metabolism, tryptophan metabolism, beta-alanine metabolism, glycerolipid metabolism, pyruvate metabolism, 1,2-dichloroethane degradation, propanoate metabolism, 3-chloroacrylic acid degradation, butanoate metabolism, and limonene and pinene degradation.

References[edit]

  • Boyer PD, Lardy H, Myrback K, eds. (1963). The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 203–221.
  • Racker E (February 1949). "Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme" (PDF). The Journal of Biological Chemistry. 177 (2): 883–92. PMID 18110463.

External links[edit]