Azot-monoksid sintaza (NAD(P)H-zavisna)
(Preusmjereno sa stranice NO synthase)
Azot-monoksid sintaza (NAD(P)H-zavisna) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.14.13.165 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Azot-monoksid sintaza (NAD(P)H-zavisna) (EC 1.14.13.165, azot suboksidna sintetaza, NO sintaza) je enzim sa sistematskim imenom L-arginin,NAD(P)H:kiseonik oksidoreduktaza (formira azot-monoksid).[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2 L-arginin + 3 NAD(P)H + 3 H+ + 4 O2 2 L-citrullin + 2 azot suboksid + 3 NAD(P)+ + 4H2O (sveukupna reakcija)
- (1a) 2 L-arginin + 2 NAD(P)H + 2 H+ + 2 O2 2 Nemega-hidroksi-L-arginin + 2 NAD(P)+ + 2H2O
- (1b) 2Nemega-hidroksi-L-arginin + NAD(P)H + H+ + 2 O2 2 L-citrullin + 2 azot suboksid + NAD(P)+ + 2H2O
Ovaj enzim vezuje hem (iron protoporfirin IX) i tetrahidrobiopterin. Većina bakterijskih i arhejskih enzima se sastoji samo od oksidaznog domena i deluje zajedno sa bakterijskim feredoksinima.
Reference[uredi | uredi kod]
- ↑ Wang, Z.Q., Lawson, R.J., Buddha, M.R., Wei, C.C., Crane, B.R., Munro, A.W. and Stuehr, D.J. (2007). „Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase”. J. Biol. Chem. 282: 2196-2202. PMID 17127770.
- ↑ Gusarov, I., Starodubtseva, M., Wang, Z.Q., McQuade, L., Lippard, S.J., Stuehr, D.J. and Nudler, E. (2008). „Bacterial nitric-oxide synthases operate without a dedicated redox partner”. J. Biol. Chem. 283: 13140-13147. PMID 18316370.
- ↑ Agapie, T., Suseno, S., Woodward, J.J., Stoll, S., Britt, R.D. and Marletta, M.A. (2009). „NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum”. Proc. Natl. Acad. Sci. USA 106: 16221-16226. PMID 19805284.
Literatura[uredi | uredi kod]
- 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.