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
Pathway
Arginine and proline metabolism
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: 
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: 
BWE: 
BWW: 
BTY: 
BMYC: 
BCL: 
BPU: 
BPUM: 
BPF: 
BMQ: 
BMD: 
BMH: 
BCO: 
BJS: 
BACI: 
BIF: 
BLE: 
BMP: 
BACW: 
BACP: 
BACB: 
BBY: 
OIH: 
GKA: 
GTE: 
GYC: 
GYA: 
GCT: 
GGH: 
AFL: 
LSP: 
LGY: 
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: 
SAUZ: 
SAB: 
SUY: 
SAUB: 
SAUM: 
SAUC: 
SAUR: 
SAUI: 
SAUT: 
SAUJ: 
SAUK: 
SAUQ: 
SAUV: 
SAUW: 
SAUX: 
SAUY: 
SAUD: 
SAUF: 
SEP: 
SER: 
SEPP: 
SEPS: 
SHA: 
SSP: 
SCA: 
SLG: 
SLN: 
SSD: 
SDT: 
SWA: 
SPAS: 
SXY: 
SXL: 
SHU: 
MCL: 
ESI: 
EAT: 
EAN: 
EXM: 
BBE: 
PJD: 
GYM: 
PPY: 
PPM: 
PPO: 
PPOL: 
PPQ: 
PTA: 
PLV: 
POD: 
PAEF: 
PAEJ: 
AAC: 
AAD: 
SIV: 
PLN: 
JEO: 
NBR: 
RHA: 
RER: 
REY: 
ROP: 
ROA: 
SMA: 
SCB: 
SVE: 
SGU: 
SVT: 
SRO: 
NML: 
SEN: 
AMD: 
AMN: 
AMM: 
AMZ: 
AOI: 
AJA: 
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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