NAD(P)Hデヒドロゲナーゼ (キノン)
NAD(P)Hデヒドロゲナーゼ (キノン) | |||||||||
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識別子 | |||||||||
EC番号 | 1.6.5.2 | ||||||||
CAS登録番号 | 9032-20-6 | ||||||||
データベース | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB構造 | RCSB PDB PDBj PDBe PDBsum | ||||||||
遺伝子オントロジー | AmiGO / QuickGO | ||||||||
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NAD(P)Hデヒドロゲナーゼ (キノン)(NAD(P)H dehydrogenase (quinone))は、次の化学反応を触媒する酸化還元酵素である。
- NAD(P)H + H+ + キノン NAD(P)+ + ヒドロキノン
反応式の通り、この酵素の基質はNADH(NADPH)とH+とキノン、生成物はNAD+(NADP+)とヒドロキノンである。補因子としてFADを用いる。
組織名はNAD(P)H:quinone oxidoreductaseで、別名に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がある。
参考文献
[編集]- 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: 455–60. 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 and Nakanishi K (Tokyo). “Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties”. J. 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: 249–258. 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: 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: 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: 8846–50. doi:10.1073/pnas.92.19.8846. PMID 7568029.