EC 1.6.5.2 - NAD(P)H dehydrogenase (quinone)

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IntEnz Enzyme Nomenclature
EC 1.6.5.2

Names

Accepted name:
NAD(P)H dehydrogenase (quinone)
Other names:
p-benzoquinone reductase
DT-diaphorase
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
dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone)
diaphorase
flavoprotein NAD(P)H-quinone reductase
menadione oxidoreductase
menadione reductase
naphthoquinone reductase
phylloquinone reductase
quinone reductase
reduced NAD(P)H dehydrogenase
reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
viologen accepting pyridine nucleotide oxidoreductase
vitamin K reductase
vitamin-K reductase
NAD(P)H2 dehydrogenase (quinone)
NQO1
QR1
Systematic name:
NAD(P)H:quinone oxidoreductase

Reactions

Cofactor

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003955
CAS Registry Number: 9032-20-6
UniProtKB/Swiss-Prot: (267) [show] [UniProt]

References

  1. di Prisco, G., Casola, L. and Giuditta, A.
    Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris.
    Biochem. J. 105: 455-460 (1967). [PMID: 4171422]
  2. Giuditta, A. and Strecker, H.J.
    Purification and some properties of a brain diaphorase.
    Biochim. Biophys. Acta 48: 10-19 (1961).
  3. Märki, F. and Martius, C.
    Vitamin K-Reductase, Darsellung und Eigenschaften.
    Biochem. Z. 333: 111-135 (1960).
  4. Misaka, E. and Nakanishi, K.
    Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties.
    J. Biochem. (Tokyo) 53: 465-471 (1963).
  5. Wosilait, W.D.
    The reduction of vitamin K1 by an enzyme from dog liver.
    J. Biol. Chem. 235: 1196-1201 (1960).
  6. Sparla, F., Tedeschi, G. and Trost, P.
    NAD(P)H:(quinone-acceptor) oxidoreductase of tobacco leaves is a flavin mononucleotide-containing flavoenzyme.
    Plant Physiol. 112: 249-258 (1996). [PMID: 12226388]
  7. Braun, M., Bungert, S. and Friedrich, T.
    Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.
    Biochemistry 37: 1861-1867 (1998). [PMID: 9485311]
  8. Jaiswal, A.K.
    Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases.
    Arch. Biochem. Biophys. 375: 62-68 (2000). [PMID: 10683249]
  9. Li, R., Bianchet, M.A., Talalay, P. and Amzel, L.M.
    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. USA 92: 8846-8850 (1995). [PMID: 7568029]

[EC 1.6.5.2 created 1961, transferred 1965 to EC 1.6.99.2, transferred 2005 to EC 1.6.5.2]