NAD(P)H dehydrogenase (quinone)

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In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction

NAD(P)H + H⁺ + a quinone $\rightleftharpoons$ NAD(P)⁺ + a hydroquinone

The 4 substrates of this enzyme are NADH, NADPH, H⁺, and quinone, whereas its 3 products are NAD⁺, NADP⁺, and hydroquinone.

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 NAD(P)H:quinone oxidoreductase. Other names in common use include menadione reductase, phylloquinone reductase, quinone reductase, dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,, quinone), DT-diaphorase, flavoprotein NAD(P)H-quinone reductase, menadione oxidoreductase, NAD(P)H dehydrogenase, NAD(P)H menadione reductase, NAD(P)H-quinone dehydrogenase, NAD(P)H-quinone oxidoreductase, NAD(P)H: (quinone-acceptor)oxidoreductase, NAD(P)H: menadione oxidoreductase, NADH-menadione reductase, naphthoquinone reductase, p-benzoquinone reductase, reduced NAD(P)H dehydrogenase, viologen accepting pyridine nucleotide oxidoreductase, vitamin K reductase, diaphorase, reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase, vitamin-K reductase, NAD(P)H2 dehydrogenase (quinone), NQO1, QR1, and NAD(P)H:(quinone-acceptor) oxidoreductase. This enzyme participates in biosynthesis of steroids. It employs one cofactor, FAD. At least one compound, Dicumarol is known to inhibit this enzyme.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2F1O.

[edit] References

IUBMB entry for 1.6.5.2
BRENDA references for 1.6.5.2 (Recommended.)
PubMed references for 1.6.5.2
PubMed Central references for 1.6.5.2
Google Scholar references for 1.6.5.2
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GIUDITTA A, STRECKER HJ (1961). "Purification and some properties of a brain diaphorase". Biochim. Biophys. Acta. 48: 10–9. doi:10.1016/0006-3002(61)90509-1. PMID 13705804.
MAERKI F, MARTIUS C (1960). "[Vitamin K reductase, preparation and properties.]". Biochem. Z. 333: 111–35. PMID 13765127.
Misaka E and Nakanishi K (Tokyo). "Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties". J. Biochem.: 465–471.
WOSILAIT WD (1960). "The reduction of vitamin K1 by an enzyme from dog liver". J. Biol. Chem. 235: 1196–201. PMID 13846011.
Sparla F, Tedeschi G, Trost P (1996). "NAD(P)H:(Quinone-Acceptor) Oxidoreductase of Tobacco Leaves Is a Flavin Mononucleotide-Containing Flavoenzyme". Plant. Physiol. 112: 249–258. PMID 12226388.
Braun M, Bungert S, Friedrich T (1998). "Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli". Biochemistry. 37: 1861–7. doi:10.1021/bi971176p. PMID 9485311.
Jaiswal AK (2000). "Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases". Arch. Biochem. Biophys. 375: 62–8. doi:10.1006/abbi.1999.1650. PMID 10683249.
Li R, Bianchet MA, Talalay P, Amzel LM (1995). "The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction". Proc. Natl. Acad. Sci. U. S. A. 92: 8846–50. doi:10.1073/pnas.92.19.8846. PMID 7568029.