| NADPH:quinone reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.6.5.5 | ||||||||
| CAS no. | 9032-20-6 | ||||||||
| 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 NADPH:quinone reductase (EC 1.6.5.5) is an enzyme that catalyzes the chemical reaction
- NADPH + H+ + 2quinone NADP+ + 2semiquinone
The 3 substrates of this enzyme are NADPH, H+, and quinone, whereas its two products are NADP+ and semiquinone.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NADPH:quinone oxidoreductase. This enzyme is also called NADPH2:quinone reductase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1IYZ, 1IZ0, and 1YB5.
References
- Rao PV, Krishna CM, Zigler JS Jr (1992). "Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase". J. Biol. Chem. 267 (1): 96–102. PMID 1370456.
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