Aldehyde dehydrogenase (NAD(P)+)

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 an acid + NAD(P)H + H+
aldehyde dehydrogenase [NAD(P)+]
Identifiers
EC no.1.2.1.5
CAS no.9028-88-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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. PMID 13319337.
    • Steinman CR, Jakoby WB (1967). "Yeast aldehyde dehydrogenase. I. Purification and crystallization". J. Biol. Chem. 242 (21): 5019–23. 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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.