NADPH—hemoprotein reduktaza

(преусмерено са EC 1.6.2.4)

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—hemoprotein reduktaza
NADPH—hemoprotein reduktaza dimer, Rattus norvegicus
Identifikatori
EC broj1.6.2.4
CAS broj2601686
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum
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 уреди

  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. & 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. & 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 уреди

Spoljašnje veze уреди