“NAD(P)H dehydrogenase (quinone)”的意思、由来-开放百科全书

词条

NAD(P)H dehydrogenase (quinone)

释义

Structural studies
References

{{enzyme
| Name = NAD(P)H dehydrogenase (quinone)
| EC_number = 1.6.5.2
| CAS_number = 9032-20-6
| IUBMB_EC_number = 1/6/5/2
| GO_code = 0003955
| image = 5f4b.jpg
| width = 270
| caption = NAD(P)H dehydrogenase (quinone) tetramer, Brucella abortus
}}

In enzymology, a NAD(P)H dehydrogenase (quinone) ({{EC number|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 {{PDB link|2F1O}}.

References

{{cite journal |vauthors=Di Prisco G, Casola L, Giuditta A | date = 1967 | title = Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris | journal = Biochem. J. | volume = 105 | pages = 455–60 | pmid = 4171422 | issue = 2 | pmc = 1198331 }}
{{cite journal |vauthors=GIUDITTA A, STRECKER HJ | date = 1961 | title = Purification and some properties of a brain diaphorase | journal = Biochim. Biophys. Acta | volume = 48 | pages = 10–9 | pmid = 13705804 | doi = 10.1016/0006-3002(61)90509-1 }}
{{cite journal |vauthors=MAERKI F, MARTIUS C | date = 1960 | title = [Vitamin K reductase, preparation and properties.] | journal = Biochem. Z. | volume = 333 | pages = 111–35 | pmid = 13765127 }}
{{cite journal |vauthors=Misaka E, Nakanishi K| location = Tokyo | title = Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties | journal = J. | volume = Biochem. | pages = 465–471 }}
{{cite journal | author = WOSILAIT WD | date = 1960 | title = The reduction of vitamin K1 by an enzyme from dog liver | journal = J. Biol. Chem. | volume = 235 | pages = 1196–201 | pmid = 13846011 }}
{{cite journal |vauthors=Sparla F, Tedeschi G, Trost P | date = 1996 | title = NAD(P)H:(Quinone-Acceptor) Oxidoreductase of Tobacco Leaves Is a Flavin Mononucleotide-Containing Flavoenzyme | journal = Plant Physiol. | volume = 112 | pages = 249–258 | pmid = 12226388 | issue = 1 | pmc = 157943 | doi = 10.1104/pp.112.1.249 }}
{{cite journal |vauthors=Braun M, Bungert S, Friedrich T | date = 1998 | title = Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli | journal = Biochemistry | volume = 37 | pages = 1861–7 | pmid = 9485311 | doi = 10.1021/bi971176p | issue = 7 }}
{{cite journal | author = Jaiswal AK | date = 2000 | title = Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases | journal = Arch. Biochem. Biophys. | volume = 375 | pages = 62–8 | pmid = 10683249 | doi = 10.1006/abbi.1999.1650 | issue = 1 }}
{{cite journal |vauthors=Li R, Bianchet MA, Talalay P, Amzel LM | date = 1995 | 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 = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | pages = 8846–50 | pmid = 7568029 | doi = 10.1073/pnas.92.19.8846 | issue = 19 | pmc = 41064 }}

5 : EC 1.6.5|NADPH-dependent enzymes|NADH-dependent enzymes|Flavin enzymes|Enzymes of known structure

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