| NADPH dehydrogenase (quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.6.5.10 | ||||||||
| CAS no. | 37256-37-4 | ||||||||
| 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 NADPH dehydrogenase (quinone) (EC 1.6.5.10) is an enzyme that catalyzes the chemical reaction
- NADPH + H+ + acceptor NADP+ + reduced acceptor
The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADPH:(quinone-acceptor) oxidoreductase. Other names in common use include reduced nicotinamide adenine dinucleotide phosphate (quinone), dehydrogenase, NADPH oxidase, and NADPH2 dehydrogenase (quinone). It has 2 cofactors: FAD, and Flavoprotein. Several compounds are known to inhibit this enzyme, including Folate, and Dicumarol.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1F5V.
See also
References
- Koli AK, Yearby C, Scott W, Donaldson KO (1969). "Purification and properties of three separate menadione reductases from hog liver". J. Biol. Chem. 244 (4): 621–9. PMID 4388793.