KEGG   ENZYME: 1.14.13.165Help
Entry
EC 1.14.13.165              Enzyme                                 

Name
nitric-oxide synthase [NAD(P)H-dependent];
nitric oxide synthetase;
NO synthase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming)
Reaction(IUBMB)
2 L-arginine + 3 NAD(P)H + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H2O (overall reaction) [RN:R00557 R10106];
(1a) 2 L-arginine + 2 NAD(P)H + 2 H+ + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O  [RN:R00558 R10107];
(1b) 2 Nomega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 = 2 L-citrulline + 2 nitric oxide + NAD(P)+ + 2 H2O [RN:R00111 R10108]
Reaction(KEGG)
Substrate
L-arginine [CPD:C00062];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007];
Nomega-hydroxy-L-arginine
Product
L-citrulline [CPD:C00327];
nitric oxide [CPD:C00533];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
Nomega-hydroxy-L-arginine
Comment
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 delta-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).
History
EC 1.14.13.165 created 2012
Reference
1  [PMID:17127770]
  Authors
Wang ZQ, Lawson RJ, Buddha MR, Wei CC, Crane BR, Munro AW, Stuehr DJ
  Title
Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.
  Journal
J. Biol. Chem. 282 (2007) 2196-202.
Reference
2  [PMID:18316370]
  Authors
Gusarov I, Starodubtseva M, Wang ZQ, McQuade L, Lippard SJ, Stuehr DJ, Nudler E
  Title
Bacterial nitric-oxide synthases operate without a dedicated redox partner.
  Journal
J. Biol. Chem. 283 (2008) 13140-7.
Reference
3  [PMID:19805284]
  Authors
Agapie T, Suseno S, Woodward JJ, Stoll S, Britt RD, Marletta MA
  Title
NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 16221-6.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system