| EC |
1.6.5.10 |
| Accepted name: |
NADPH dehydrogenase (quinone) |
| Reaction: |
NADPH + H+ + a quinone = NADP+ + a quinol |
| Other name(s): |
reduced nicotinamide adenine dinucleotide phosphate (quinone) dehydrogenase; NADPH oxidase; NADPH2 dehydrogenase (quinone) |
| Systematic name: |
NADPH:(quinone-acceptor) oxidoreductase |
| Comments: |
A flavoprotein [1, 2]. The enzyme from Escherichia coli is specific for NADPH and is most active with quinone derivatives and ferricyanide as electron acceptors [3].
Menaquinone can act as acceptor. The enzyme from hog liver is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-37-4 |
| References: |
| 1. |
Koli, A.K., Yearby, C., Scott, W. and Donaldson, K.O. Purification and properties of three separate menadione reductases from hog liver. J. Biol. Chem. 244 (1969) 621–629. [PMID: 4388793] |
| 2. |
Hayashi, M., Hasegawa, K., Oguni, Y. and Unemoto, T. Characterization of FMN-dependent NADH-quinone reductase induced by menadione in Escherichia coli. Biochim. Biophys. Acta 1035 (1990) 230–236. [DOI] [PMID: 2118386] |
| 3. |
Hayashi, M., Ohzeki, H., Shimada, H. and Unemoto, T. NADPH-specific quinone reductase is induced by 2-methylene-4-butyrolactone in Escherichia coli. Biochim. Biophys. Acta 1273 (1996) 165–170. [DOI] [PMID: 8611590] |
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| [EC 1.6.5.10 created 1972 as EC 1.6.99.6, transferred 2011 to EC 1.6.5.10] |
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