NAD(P)H dehydrogenase (quinone);
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;
NAD(P)H:(quinone-acceptor) oxidoreductase

Oxidoreductases;
Acting on NADH or NADPH;
With a quinone or similar compound as acceptor

NAD(P)H:quinone oxidoreductase

NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone [RN:R07358 R07359]

R07358 > R02964 R03643 R03816;
R07359

NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
quinone [CPD:C00472]

A flavoprotein. The enzyme catalyses a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone [6]. The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.

1  [PMID:4171422]

Di Prisco G, Casola L, Giuditta A.

Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris.

Biochem. J. 105 (1967) 455-60.

Octopus vulgaris

2  [PMID:13705804]

GIUDITTA A, STRECKER HJ.

Purification and some properties of a brain diaphorase.

Biochim. Biophys. Acta. 48 (1961) 10-9.

Bos taurus [GN:bta]

3  [PMID:13765127]

MAERKI F, MARTIUS C.

[Vitamin K reductase, preparation and properties.]

Biochem. Z. 333 (1960) 111-35.

4

Misaka, E. and Nakanishi, K.

Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties.

J. Biochem. (Tokyo) 53 (1963) 465-471.

5  [PMID:13846011]

WOSILAIT WD.

The reduction of vitamin K1 by an enzyme from dog liver.

J. Biol. Chem. 235 (1960) 1196-201.

Canis familiaris [GN:cfa]

6  [PMID:12226388]

Sparla F, Tedeschi G, Trost P.

NAD(P)H:(Quinone-Acceptor) Oxidoreductase of Tobacco Leaves Is a Flavin Mononucleotide-Containing Flavoenzyme.

Plant. Physiol. 112 (1996) 249-258.

Nicotiana tabacum

7  [PMID:9485311]

Braun M, Bungert S, Friedrich T.

Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.

Biochemistry. 37 (1998) 1861-7.

Escherichia coli [GN:eco]

8  [PMID:10683249]

Jaiswal AK.

Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases.

Arch. Biochem. Biophys. 375 (2000) 62-8.

Rattus norvegicus [GN:rno]

9  [PMID:7568029]

Li R, Bianchet MA, Talalay P, Amzel LM.

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 (1995) 8846-50.

Rattus norvegicus [GN:rno]