NAD(P)H dehydrogenase (quinone)

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NAD(P)H dehydrogenase (quinone)
5f4b.jpg
NAD(P)H dehydrogenase (quinone) tetramer, Brucella abortus
Identifiers
EC number1.6.5.2
CAS number9032-20-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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 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.

Structural studies[edit]

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

References[edit]

  • Di Prisco G, Casola L, Giuditta A (1967). "Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris". Biochem. J. 105 (2): 455–60. PMC 1198331. PMID 4171422.
  • 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, Nakanishi K. "Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties". J. Tokyo. 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 (1): 249–258. doi:10.1104/pp.112.1.249. PMC 157943. 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 (7): 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 (1): 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 (19): 8846–50. doi:10.1073/pnas.92.19.8846. PMC 41064. PMID 7568029.