Aldehyde dehydrogenase (NAD(P)+)

aldehyde dehydrogenase [NAD(P)+]
Identifiers
EC no.	1.2.1.5
CAS no.	9028-88-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) is an enzyme that catalyzes the chemical reaction

an aldehyde + NAD(P)+ + H₂O ${\displaystyle \rightleftharpoons }$ an acid + NAD(P)H + H^+

The 4 substrates of this enzyme are aldehyde, NAD^+, NADP^+, and H₂O, whereas its 4 products are acid, NADH, NADPH, 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(P)+ oxidoreductase. Other names in common use include aldehyde dehydrogenase [NAD(P)+], and ALDH. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, and metabolism of xenobiotics by cytochrome p450.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1AD3, 1EYY, 1EZ0, and 2AMF.

References

• Black S (1951). "Yeast aldehyde dehydrogenase". Arch. Biochem. Biophys. 34 (1): 86–97. doi:10.1016/S0003-9861(51)80013-4. PMID 14904038.
• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
• KING TE, CHELDELIN VH (1956). "Oxidation of acetaldehyde by Acetobacter suboxydans". J. Biol. Chem. 220 (1): 177–91. doi:10.1016/S0021-9258(18)65343-8. PMID 13319337.
• Steinman CR, Jakoby WB (1967). "Yeast aldehyde dehydrogenase. I. Purification and crystallization". J. Biol. Chem. 242 (21): 5019–23. doi:10.1016/S0021-9258(18)99471-8. PMID 4293780.
• Tanenbaum SW (1956). "The metabolism of Acetobacter peroxidans. I. Oxidative enzymes". Biochim. Biophys. Acta. 21 (2): 335–342. doi:10.1016/0006-3002(56)90017-8. PMID 13363916.