| Aldehyde dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.4 | ||||||||
| CAS no. | 9028-87-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, an aldehyde dehydrogenase (NADP+) ( EC 1.2.1.4) is an enzyme that catalyzes the chemical reaction
- an aldehyde + NADP+ + H2O 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. Biochem. Tokyo: 812–830.
- SEEGMILLER JE (1953). "Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast". J. Biol. Chem. 201 (2): 629–37. PMID 13061400.
