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Nitric-oxide synthase (NAD(P)H-dependent) (EC 1.14.14.47, nitric oxide synthetase, NO synthase) is an enzyme with systematic name L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming). This enzyme catalyses the following chemical reaction

2 L-arginine + 3 NAD(P)H + 3 H + 4 O₂ ${\displaystyle \rightleftharpoons }$ 2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H₂O (overall reaction)

(1a) 2 L-arginine + 2 NAD(P)H + 2 H + 2 O₂ ${\displaystyle \rightleftharpoons }$ 2 N-omega-hydroxy-L-arginine + 2 NAD(P) + 2 H₂O

(1b) 2 N-omega-hydroxy-L-arginine + NAD(P)H + H + 2 O₂ ${\displaystyle \rightleftharpoons }$ 2 L-citrulline + 2 nitric oxide + NAD(P) + 2 H₂O

Nitric-oxide synthase (NAD(P)H-dependent) binds heme (iron protoporphyrin IX) and tetrahydrobiopterin.

See also

• Nitric oxide synthase

References

1. Wang ZQ, Lawson RJ, Buddha MR, Wei CC, Crane BR, Munro AW, Stuehr DJ (January 2007). "Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase". The Journal of Biological Chemistry. 282 (4): 2196–202. doi:10.1074/jbc.M608206200. PMID 17127770.
2. Gusarov I, Starodubtseva M, Wang ZQ, McQuade L, Lippard SJ, Stuehr DJ, Nudler E (May 2008). "Bacterial nitric-oxide synthases operate without a dedicated redox partner". The Journal of Biological Chemistry. 283 (19): 13140–7. doi:10.1074/jbc.M710178200. PMC 2442334. PMID 18316370.
3. Agapie T, Suseno S, Woodward JJ, Stoll S, Britt RD, Marletta MA (September 2009). "NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum". Proceedings of the National Academy of Sciences of the United States of America. 106 (38): 16221–6. doi:10.1073/pnas.0908443106. PMC 2752531. PMID 19805284.

External links

• Nitric-oxide+synthase+(NAD(P)H-dependent) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 1.14.13