NAD(P)H dehydrogenase (quinone)

NAD(P)H dehydrogenase (quinone)

NAD(P)H dehydrogenase (quinone) tetramer, Brucella abortus
Identifiers
EC number 1.6.5.2
CAS number 9032-20-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

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

References


    This article is issued from Wikipedia - version of the 9/13/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.