Azot-monoksid sintaza

Azot-monoksid sintaza
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
Pretraga PMC articles PubMed articles NCBI Protein search

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 ${\displaystyle \rightleftharpoons }$ 2 L-citrulin + 2 azot suboksid + 3 NADP⁺ + 4H₂O (sveukupna reakcija)

(1a) 2 L-arginin + 2 NADPH + 2 H⁺ + 2 O₂ ${\displaystyle \rightleftharpoons }$ 2 Nomega-hidroksi-L-arginin + 2 NADP⁺ + 2H₂O

(1b) 2 Nomega-hidroksi-L-arginin + NADPH + H⁺ + 2 O₂ ${\displaystyle \rightleftharpoons }$ 2 L-citrulin + 2 azot suboksid + NADP⁺ + 2H₂O

Ovaj enzim vezuje FAD, FMN, hem (gvožđe protoporfirin IX) i tetrahidrobiopterin.

Reference

1. 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. 
2. Stuehr, D.J., Kwon, N.S., Nathan, C.F., Griffith, O.W., Feldman, P.L. and Wiseman, J. (1991). „N^ω-hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-arginine”. J. Biol. Chem. 266: 6259-6263. PMID 1706713. 
3. Stuehr, D., Pou, S. and Rosen, G.M. (2001). „Oxygen reduction by nitric-oxide synthases”. J. Biol. Chem. 276: 14533-14536. PMID 11279231. 
4. 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)