IUBMB Enzyme Nomenclature

EC 1.14.13.165

Accepted name: nitric-oxide synthase [NAD(P)H-dependent]

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 Nω-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
(1b) 2 Nω-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 = 2 L-citrulline + 2 nitric oxide + NAD(P)+ + 2 H2O

Other name(s): nitric oxide synthetase; NO synthase

Systematic name: L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming)

Comments: Binds heme (iron protoporphyrin IX) and tetrahydrobiopterin. Most of the bacterial and archaeal enzymes consist of only an oxidase domain and function together with bacterial ferredoxins [1-2]. The enzyme from the δ-proteobacterium Sorangium cellulosum also includes a reductase domain that binds FAD, FMN and a [2Fe-2S] cluster [3]. The similar enzymes from plants and animals use only NADPH as acceptor (cf. EC 1.14.13.39).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wang, Z.Q., Lawson, R.J., Buddha, M.R., Wei, C.C., Crane, B.R., Munro, A.W. and Stuehr, D.J. Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase. J. Biol. Chem. 282 (2007) 2196-2202. [PMID: 17127770]

2. Gusarov, I., Starodubtseva, M., Wang, Z.Q., McQuade, L., Lippard, S.J., Stuehr, D.J. and Nudler, E. Bacterial nitric-oxide synthases operate without a dedicated redox partner. J. Biol. Chem. 283 (2008) 13140-13147. [PMID: 18316370]

3. Agapie, T., Suseno, S., Woodward, J.J., Stoll, S., Britt, R.D. and Marletta, M.A. NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum. Proc. Natl. Acad. Sci. USA 106 (2009) 16221-16226. [PMID: 19805284]

[EC 1.14.13.165 created 2012]


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