| glycerol dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.72 | ||||||||
| CAS no. | 37250-11-6 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glycerol dehydrogenase (NADP+) (EC 1.1.1.72) is an enzyme that catalyzes the chemical reaction
- glycerol + NADP+ D-glyceraldehyde + NADPH + H+
Thus, the two substrates of this enzyme are glycerol and NADP+, whereas its 3 products are D-glyceraldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycerol:NADP+ oxidoreductase. This enzyme is also called glycerol dehydrogenase (NADP+). This enzyme participates in glycerolipid metabolism.
References
- Kormann AW, Hurst RO, Flynn TG (1972). "Purification and properties of an NADP+-dependent glycerol dehydrogenase from rabbit skeletal muscle". Biochim. Biophys. Acta. 258 (1): 40–55. doi:10.1016/0005-2744(72)90965-5. PMID 4400494.
- Toews CJ (1967). "The kinetics and reaction mechanism of the nicotinamide-adinine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle". Biochem. J. 105 (3): 1067–1073. PMC 1198427. PMID 16742532.
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