Aldehyde dehydrogenase (NADP+)

In enzymology, an aldehyde dehydrogenase (NADP+) (EC 1.2.1.4) is an enzyme that catalyzes the chemical reaction

an aldehyde + NADP⁺ + H₂O ${\displaystyle \rightleftharpoons }$ an acid + NADPH + H⁺

The 3 substrates of this enzyme are aldehyde, NADP⁺, and H₂O, whereas its 3 products are acid, 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:NADP+ oxidoreductase. Other names in common use include NADP+-acetaldehyde dehydrogenase, NADP+-dependent aldehyde dehydrogenase, and aldehyde dehydrogenase (NADP+). This enzyme participates in caprolactam degradation.

References

• Adachi O, Matsushita K, Shinagawa E, Ameyama M (1980). "Crystallization and properties of NADP-dependent aldehyde dehydrogenase from Gluconobacter melanogenus". Agric. Biol. Chem. 44: 155–164. doi:10.1271/bbb1961.44.155.
• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
• Nakayama T. "Acetic acid bacteria. II. Intracellular distribution of enzymes related to acetic acid fermentation, and some properties of a highly purified triphosphopyridine nucleotide (TPN)-dependent aldehyde dehydrogenase". J. Tokyo. Biochem.: 812–830.
• SEEGMILLER JE (1953). "Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast". J. Biol. Chem. 201 (2): 629–37. PMID 13061400.

This page was last edited on 26 August 2023, at 13:02