Azot-monoksid sintaza
| Azot-monoksid sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Prikaz baziran na 1nsi | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.14.13.39 | ||||||||
| CAS broj | 125978-95-2 | ||||||||
| 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 (EC 1.14.13.39, azot suboksidna sintetaza, NO sintaza, NADPH-dijaforaza) je enzim sa sistematskim imenom L-arginin,NADPH:kiseonik oksidoreduktaza (formira azot suboksid).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2 L-arginin + 3 NADPH + 3 H+ + 4 O2 2 L-citrulin + 2 azot suboksid + 3 NADP+ + 4H2O (sveukupna reakcija)
- (1a) 2 L-arginin + 2 NADPH + 2 H+ + 2 O2 2 Nomega-hidroksi-L-arginin + 2 NADP+ + 2H2O
- (1b) 2 Nomega-hidroksi-L-arginin + NADPH + H+ + 2 O2 2 L-citrulin + 2 azot suboksid + NADP+ + 2H2O
Ovaj enzim vezuje FAD, FMN, hem (gvožđe protoporfirin IX) i tetrahidrobiopterin.
Reference
- ↑ Bredt, D.S. and Snyder, S.H. (1990). „Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme”. Proc. Natl. Acad. Sci. USA 87: 682-685. PMID 1689048.
- ↑ Stuehr, D.J., Kwon, N.S., Nathan, C.F., Griffith, O.W., Feldman, P.L. and Wiseman, J. (1991). „Nω-hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-arginine”. J. Biol. Chem. 266: 6259-6263. PMID 1706713.
- ↑ Stuehr, D., Pou, S. and Rosen, G.M. (2001). „Oxygen reduction by nitric-oxide synthases”. J. Biol. Chem. 276: 14533-14536. PMID 11279231.
- ↑ Foresi, N., Correa-Aragunde, N., Parisi, G., Calo, G., Salerno, G. and Lamattina, L. (2010). „Characterization of a nitric oxide synthase from the plant kingdom: NO generation from the green alga Ostreococcus tauri is light irradiance and growth phase dependent”. Plant Cell 22: 3816-3830. PMID 21119059.
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.
Vanjske veze
- MeSH Nitric-oxide+synthase+(NADPH+dependent)
- 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
