KEGG   ENZYME: 1.14.13.165Help
Entry
EC 1.14.13.165              Enzyme                                 

Name
nitric-oxide synthase [NAD(P)H];
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
Pathway
Arginine and proline metabolism
Metabolic pathways
Biosynthesis of antibiotics
Orthology
K00491  
nitric-oxide synthase, bacterial
Genes
SCL: 
sce1582(nos)
SCU: 
BSU: 
BSU07630(nosA)
BSR: 
BSL: 
BSH: 
BSY: 
BSUT: 
BSUL: 
BSUS: 
BSS: 
BST: 
BSO: 
BSN: 
BSQ: 
BSX: 
BSP: 
BLI: 
BL03064(nos)
BLD: 
BLH: 
BAO: 
BAY: 
BAQ: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_0759(nosA)
BAMN: 
BASU_0734(nosA)
BAMB: 
BAMT: 
BAZ: 
BQL: 
BXH: 
BQY: 
BAMI: 
BAMC: 
BAMF: 
BAMY: 
BAE: 
BATR: 
BHA: 
BAN: 
BAR: 
BAT: 
BAH: 
BAI: 
BAX: 
BANT: 
BANR: 
BANS: 
BANH: 
BANV: 
BAL: 
BCE: 
BCA: 
BCZ: 
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCX: 
BNC: 
BCF: 
BCER: 
BCEF: 
BCY: 
BTK: 
BTL: 
BTB: 
BTT: 
BTHR: 
BTHI: 
BTC: 
BTF: 
BTM: 
MC28_4678(rplB)
BTG: 
BTI: 
BTN: 
BTHT: 
BTHU: 
BTW: 
BWE: 
BWW: 
BTY: 
BMYC: 
BMYO: 
BCL: 
BPU: 
BPUM: 
BPF: 
BMQ: 
BMD: 
BMH: 
BMEG: 
BCO: 
BJS: 
BACI: 
BIF: 
BLE: 
BMP: 
BACW: 
BACP: 
BACB: 
BBY: 
BACY: 
BACL: 
OIH: 
GKA: 
GTE: 
GYC: 
GYA: 
GCT: 
GGH: 
AFL: 
LSP: 
LGY: 
LFU: 
HHD: 
TAP: 
BSE: 
SAU: 
SAV: 
SAW: 
SAH: 
SAJ: 
SAM: 
SAS: 
SAR: 
SAC: 
SAX: 
SAA: 
SAO: 
SAE: 
SAD: 
SUU: 
SUV: 
SUH: 
SUE: 
SUJ: 
SUK: 
SUC: 
SUT: 
SUQ: 
SUZ: 
SUD: 
SUX: 
SUW: 
SUG: 
SUF: 
SAUA: 
SAUE: 
SAUN: 
SAUS: 
SAUU: 
SAUG: 
SAUZ: 
SAB: 
SUY: 
SAUB: 
SAUM: 
SAUC: 
SAUR: 
SAUI: 
SAUT: 
SAUJ: 
SAUK: 
SAUQ: 
SAUV: 
SAUW: 
SAUX: 
SAUY: 
SAUD: 
SAUF: 
SEP: 
SER: 
SEPP: 
SEPS: 
SHA: 
SHH: 
SSP: 
SCA: 
SLG: 
SLN: 
SSD: 
SDT: 
SWA: 
SPAS: 
SXY: 
SXL: 
SXO: 
SHU: 
MCL: 
ESI: 
EAT: 
EAN: 
EXM: 
BBE: 
PJD: 
GYM: 
PPY: 
PPM: 
PPO: 
PPOL: 
PPQ: 
PPOY: 
PTA: 
PLV: 
POD: 
PAEF: 
PAEJ: 
PIH: 
AAC: 
AAD: 
SIV: 
PLN: 
JEO: 
NBR: 
RHA: 
RER: 
REY: 
REB: 
ROP: 
ROA: 
SMA: 
SCB: 
SVE: 
SGU: 
SVT: 
SRO: 
NML: 
SEN: 
AMD: 
AMN: 
AMM: 
AMZ: 
AOI: 
AJA: 
ALU: 
PDX: 
AMI: 
SESP: 
KAL: 
SAQ: 
AMS: 
ASE: 
ACTN: 
AFS: 
CAI: 
CEP: 
MIC: 
ANB: 
DRA: 
DGE: 
DDR: 
DMR: 
DPT: 
DGO: 
DPD: 
NPH: 
NP1908A(nos)
NGE: 
 » show all
Taxonomy
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: 

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