In enzymology, a glycerol dehydrogenase (NADP ) (EC 1.1.1.72) is an enzyme that catalyzes the chemical reaction
glycerol dehydrogenase (NADP ) | |||||||||
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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 | ||||||||
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- 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
edit- 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 4400494.40-55&rft.date=1972&rft_id=info:doi/10.1016/0005-2744(72)90965-5&rft_id=info:pmid/4400494&rft.aulast=Kormann&rft.aufirst=AW&rft.au=Hurst, RO&rft.au=Flynn, TG&rfr_id=info:sid/en.wikipedia.org:Glycerol dehydrogenase (NADP+)" class="Z3988">
- 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 16742532.1067-1073&rft.date=1967&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1198427#id-name=PMC&rft_id=info:pmid/16742532&rft.au=Toews CJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1198427&rfr_id=info:sid/en.wikipedia.org:Glycerol dehydrogenase (NADP+)" class="Z3988">