| Entry |
|
|---|
| 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
|
|---|
| Class |
Oxidoreductases;
Acting on NADH or NADPH;
With a quinone or similar compound as acceptor
 |
|---|
| Sysname |
NAD(P)H:quinone oxidoreductase
|
|---|
| Reaction(IUBMB) |
NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone [RN: R07358 R07359]
|
|---|
| Reaction(KEGG) |
|
|---|
| Substrate |
|
|---|
| Product |
|
|---|
| 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.
|
|---|
| History |
EC 1.6.5.2 created 1961, transferred 1965 to EC 1.6.99.2, transferred 2005 to EC 1.6.5.2
|
|---|
| Pathway |
| ec00130 | Ubiquinone and other terpenoid-quinone biosynthesis |
| ec01110 | Biosynthesis of secondary metabolites |
|
|---|
| Orthology |
| K00355 | NAD(P)H dehydrogenase (quinone) |
| K03809 | NAD(P)H dehydrogenase (quinone) |
| K19267 | NAD(P)H dehydrogenase (quinone) |
|
|---|
| Genes |
» show all
 |
|---|
| Reference |
|
|---|
| 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 |
|
|---|
| Authors |
GIUDITTA A, STRECKER HJ. |
|---|
| Title |
Purification and some properties of a brain diaphorase. |
|---|
| Journal |
|
|---|
| Reference |
|
|---|
| 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 |
|
|---|
| Authors |
WOSILAIT WD. |
|---|
| Title |
The reduction of vitamin K1 by an enzyme from dog liver. |
|---|
| Journal |
J Biol Chem 235:1196-201 (1960) |
|---|
| Reference |
|
|---|
| 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 |
|
|---|
| 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 |
|
|---|
| Reference |
|
|---|
| Authors |
Jaiswal AK. |
|---|
| Title |
Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases. |
|---|
| Journal |
|
|---|
| Reference |
|
|---|
| 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 |
|
|---|
| Sequence |
|
|---|
| 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 |
|
|---|
