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
- ↑ 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.
- ↑ Horecker, B.L. (1950). „Triphosphopyridine nucleotide-cytochrome c reductase in liver”. J. Biol. Chem. 183: 593-605.
- ↑ 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.
- ↑ 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.
- ↑ Williams, C.H., Jr. and Kamin, H. (1962). „Microsomal triphosphopyridine nucleotide-cytochrome c reductase in liver”. J. Biol. Chem. 237: 587-595. PMID 14007123.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH NADPH---hemoprotein+reductase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
