Entry |
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Name |
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
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Class |
Oxidoreductases;
Acting on NADH or NADPH;
With a quinone or similar compound as acceptor
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Sysname |
NAD(P)H:quinone oxidoreductase
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Reaction(IUBMB) |
NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone [RN: R07358 R07359]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
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.
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History |
EC 1.6.5.2 created 1961, transferred 1965 to EC 1.6.99.2, transferred 2005 to EC 1.6.5.2
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Pathway |
ec00130 | Ubiquinone and other terpenoid-quinone biosynthesis |
ec01110 | Biosynthesis of secondary metabolites |
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Orthology |
K00355 | NAD(P)H dehydrogenase (quinone) |
K03809 | NAD(P)H dehydrogenase (quinone) |
K19267 | NAD(P)H dehydrogenase (quinone) |
K23842 | NAD(P)H dehydrogenase (quinone) |
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Genes |
» show all
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Reference |
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Authors |
Di Prisco G, Casola L, Giuditta A. |
Title |
Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris. |
Journal |
Biochem J 105:455-60 (1967) |
Reference |
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Authors |
GIUDITTA A, STRECKER HJ. |
Title |
Purification and some properties of a brain diaphorase. |
Journal |
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Reference |
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Authors |
MAERKI F, MARTIUS C. |
Title |
[Vitamin K reductase, preparation and properties.] |
Journal |
Biochem Z 333:111-35 (1960) |
Reference |
4 |
Authors |
Misaka, E. and Nakanishi, K. |
Title |
Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties. |
Journal |
J Biochem (Tokyo) 53:465-471 (1963) |
Reference |
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Authors |
WOSILAIT WD. |
Title |
The reduction of vitamin K1 by an enzyme from dog liver. |
Journal |
J Biol Chem 235:1196-201 (1960) |
Reference |
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Authors |
Sparla F, Tedeschi G, Trost P. |
Title |
NAD(P)H:(Quinone-Acceptor) Oxidoreductase of Tobacco Leaves Is a Flavin Mononucleotide-Containing Flavoenzyme. |
Journal |
Plant Physiol 112:249-258 (1996) |
Reference |
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Authors |
Braun M, Bungert S, Friedrich T. |
Title |
Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. |
Journal |
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Reference |
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Authors |
Jaiswal AK. |
Title |
Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases. |
Journal |
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Reference |
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Authors |
Li R, Bianchet MA, Talalay P, Amzel LM. |
Title |
The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.6.5.2 |
ExPASy - ENZYME nomenclature database: | 1.6.5.2 |
BRENDA, the Enzyme Database: | 1.6.5.2 |
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