Nitric-oxide synthase (NAD(P)H-dependent)

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Nitric-oxide synthase (NAD(P)H-dependent)
Identifiers
EC number1.14.14.47
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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).[1][2][3] This enzyme catalyses the following chemical reaction

2 L-arginine + 3 NAD(P)H + 3 H+ + 4 O2 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 2 N-omega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
(1b) 2 N-omega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 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[edit]

References[edit]

  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.

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