“NADPH—hemoprotein reductase”的意思、由来-开放百科全书

词条

NADPH—hemoprotein reductase

释义

Structural studies
References

{{enzyme
| Name = NADPH—hemoprotein reductase
| EC_number = 1.6.2.4
| CAS_number = 9023-03-4
| IUBMB_EC_number = 1/6/2/4
| GO_code = 0003958
| image = 1j9z.jpg
| width = 270
| caption = NADPH-Cytochrome P450 reductase dimer, Rattus norvegicus
}}

In enzymology, a NADPH—hemoprotein reductase ({{EC number|1.6.2.4}}) is an enzyme that catalyzes the chemical reaction

NADPH + H⁺ + n oxidized hemoprotein NADP⁺ + n reduced hemoprotein

The 3 substrates of this enzyme are NADPH, H⁺, and oxidized hemoprotein, whereas its two products are NADP⁺ and reduced hemoprotein.

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NADPH:hemoprotein oxidoreductase. Other names in common use include CPR, FAD-cytochrome c reductase, NADP---cytochrome c reductase, NADP---cytochrome reductase, NADPH-dependent cytochrome c reductase, NADPH:P-450 reductase, NADPH:ferrihemoprotein oxidoreductase, NADPH---cytochrome P-450 oxidoreductase, NADPH---cytochrome c oxidoreductase, NADPH---cytochrome c reductase, NADPH---cytochrome p-450 reductase, NADPH---ferricytochrome c oxidoreductase, NADPH---ferrihemoprotein reductase, TPNH2 cytochrome c reductase, TPNH-cytochrome c reductase, aldehyde reductase (NADPH-dependent), cytochrome P-450 reductase, cytochrome c reductase (reduced nicotinamide adenine dinucleotide, phosphate, NADPH, NADPH-dependent), dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c, reductase, ferrihemoprotein P-450 reductase, reduced nicotinamide adenine dinucleotide phosphate-cytochrome c, reductase, reductase, cytochrome c (reduced nicotinamide adenine dinucleotide, and phosphate). It has 2 cofactors: FAD, and FMN.

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1AMO}}, {{PDB link|1B1C}}, {{PDB link|1J9Z}}, {{PDB link|1JA0}}, {{PDB link|1JA1}}, {{PDB link|1YQO}}, {{PDB link|1YQP}}, {{PDB link|2BF4}}, {{PDB link|2BN4}}, and {{PDB link|2BPO}}.

References

{{cite journal |vauthors=Haas E, Horecker BL, Hogness TR | year = 1940 | title = The enzymatic reduction of cytochrome c, cytochrome c reductase | journal = J. Biol. Chem. | volume = 136 | pages = 747–774 }}
{{cite journal | author = Horecker BL | year = 1950 | title = Triphosphopyridine nucleotide-cytochrome c reductase in liver | journal = J. Biol. Chem. | volume = 183 | pages = 593–605 }}
{{cite journal |vauthors=Lu AY, Junk KW, Coon MJ | year = 1969 | title = Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components | journal = J. Biol. Chem. | volume = 244 | pages = 3714–21 | pmid = 4389465 | issue = 13 }}
{{cite journal |vauthors=GIBSON QH, PALMER G, WHARTON DC | year = 1965 | title = STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE | journal = J. Biol. Chem. | volume = 240 | pages = 921–31 | pmid = 14275154 }}
{{cite journal |author1=WILLIAMS CH Jr |author2=KAMIN H | year = 1962 | title = Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver | journal = J. Biol. Chem. | volume = 237 | pages = 587–95 | pmid = 14007123 }}
{{cite journal |vauthors=Masters BS, Bilimoria MH, Kamin H, Gibson QH | year = 1965 | title = The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase | journal = J. Biol. Chem. | volume = 240 | pages = 4081–8 | pmid = 4378860 | issue = 10 }}
{{cite journal |vauthors=Sevrioukova IF, Peterson JA | year = 1995 | title = NADPH-P-450 reductase: structural and functional comparisons of the eukaryotic and prokaryotic isoforms | journal = Biochimie | volume = 77 | pages = 562–72 | pmid = 8589067 | doi = 10.1016/0300-9084(96)88172-7 | issue = 7-8 }}
{{cite journal |vauthors=Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ | year = 1997 | title = Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | pages = 8411–6 | pmid = 9237990 | doi = 10.1073/pnas.94.16.8411 | issue = 16 | pmc = 22938 }}
{{cite journal |vauthors=Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK | year = 2001 | title = Determination of the redox properties of human NADPH-cytochrome P450 reductase | journal = Biochemistry | volume = 40 | pages = 1956–63 | pmid = 11329262 | doi = 10.1021/bi001718u | issue = 7 }}
{{cite journal |vauthors=Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK | year = 2001 | title = Determination of the redox properties of human NADPH-cytochrome P450 reductase | journal = Biochemistry | volume = 40 | pages = 1956–63 | pmid = 11329262 | doi = 10.1021/bi001718u | issue = 7 }}
{{cite journal | author = Scrutton NS | year = 2003 | title = Electron transfer in human cytochrome P450 reductase | journal = Biochem. Soc. Trans. | volume = 31 | pages = 497–501 | pmid = 12773143 | doi = 10.1042/BST0310497 | last2 = Grunau | first2 = A | last3 = Paine | first3 = M | last4 = Munro | first4 = AW | last5 = Wolf | first5 = CR | last6 = Roberts | first6 = GC | last7 = Scrutton | first7 = NS | issue = Pt 3 }}
{{cite journal | author = Scrutton NS | year = 2003 | title = Electron transfer in human cytochrome P450 reductase | journal = Biochem. Soc. Trans. | volume = 31 | pages = 497–501 | pmid = 12773143 | doi = 10.1042/BST0310497 | last2 = Grunau | first2 = A | last3 = Paine | first3 = M | last4 = Munro | first4 = AW | last5 = Wolf | first5 = CR | last6 = Roberts | first6 = GC | last7 = Scrutton | first7 = NS | issue = Pt 3 }}

{{NADH or NADPH oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{DEFAULTSORT:NADPH-hemoprotein reductase}}{{1.6-enzyme-stub}}

4 : EC 1.6.2|NADPH-dependent enzymes|Flavin enzymes|Enzymes of known structure

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