NADPH—hemoprotein reduktaza

NADPH—hemoprotein reduktaza
NADPH—hemoprotein reduktaza dimer, Rattus norvegicus
Identifikatori
EC broj 1.6.2.4
CAS broj 2601686
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

NADPH—hemoprotein reduktaza (EC 1.6.2.4, CPR, FAD-citohrom c reduktaza, NADP---citohrom c reduktaza, NADP---citohrom reduktaza, NADPH-zavisna citohrom c reduktaza, NADPH:P-450 reduktaza, NADPH:ferihemoproteinska oksidoreduktaza, NADPH---citohrom P-450 oksidoreduktaza, NADPH---citohrom c oksidoreduktaza, NADPH---citohrom c reduktaza, NADPH---citohrom p-450 reduktaza, NADPH---fericitohrom c oksidoreduktaza, NADPH---ferihemoproteinska reduktaza, TPNH2 citohrom c reduktaza, TPNH-citohrom c reduktaza, aldehidna reduktaza (NADPH-zavisna), citohrom P-450 reduktaza, citohrom c reduktaza, dihidroksinikotinamid adenin dinukleotid fosfat-citohrom c reduktaza, ferihemoprotein P-450 reduktaza, redukovani nikotinamid adenin dinukleotid fosfat-citohrom c reduktaza, reduktaza, citohrom c (redukovani nikotinamid adenin dinukleotid fosfat)) je enzim sa sistematskim imenom NADPH:hemoprotein oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

NADPH + H+ + n oksidovani hemoprotein NADP+ + n redukovani hemoprotein

Ovaj enzim je flavoprotein (FMN, FAD) koji sadrži FMN i FAD. Broj n u jednačini je 1 ako hemoprotein podleže dvoelektronskoj redukciji, a njegova vrednost je 2 pri jednoelektronskoj redukciji.

Reference

  1. ↑ Haas, E., Horecker, B.L. and Hogness, T.R. (1940). „The enzymatic reduction of cytochrome c, cytochrome c reductase”. J. Biol. Chem. 136: 747-774. 
  2. ↑ Horecker, B.L. (1950). „Triphosphopyridine nucleotide-cytochrome c reductase in liver”. J. Biol. Chem. 183: 593-605. 
  3. ↑ Lu, A.Y.H., Junk, K.W. and Coon, M.J. (1969). „Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components”. J. Biol. Chem. 244: 3714-3721. PMID 4389465. 
  4. ↑ Masters, B.S.S., Kamin, H., Gibson, Q.H. and Williams, C.H., Jr. (1965). „Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase”. J. Biol. Chem. 240: 921-931. PMID 14275154. 
  5. ↑ Williams, C.H., Jr. and Kamin, H. (1962). „Microsomal triphosphopyridine nucleotide-cytochrome c reductase in liver”. J. Biol. Chem. 237: 587-595. PMID 14007123. 
  6. ↑ Masters, B.S.S., Bilimoria, M.H, Kamen, H. and Gibson, Q.H. (1965). „The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase”. J. Biol. Chem. 240: 4081-4088. PMID 4378860. 
  7. ↑ Sevrioukova, I.F. and Peterson, J.A. (1995). „NADPH-P-450 reductase: Structural and functional comparisons of the eukaryotic and prokaryotic isoforms”. Biochimie 77: 562-572. PMID 8589067. 
  8. ↑ Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S.S. and Kim, J.-J.P. (1997). „Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes”. Proc. Natl. Acad. Sci. USA 94: 8411-8416. PMID 9237990. 
  9. ↑ Munro, A.W., Noble, M.A., Robledo, L., Daff, S.N. and Chapman, S.K. (2001). „Determination of the redox properties of human NADPH-cytochrome P450 reductase”. Biochemistry 40: 1956-1963. PMID 11329262. 
  10. ↑ Gutierrez, A., Grunau, A., Paine, M., Munro, A.W., Wolf, C.R., Roberts, G.C.K. and Scrutton, N.S. (2003). „Electron transfer in human cytochrome P450 reductase”. Biochem. Soc. Trans. 31: 497-501. PMID 12773143. 

Literatura

Vanjske veze