PMID:7528745

Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA

Structural organization of the human neuronal nitric oxide synthase gene (NOS1).

J Biol Chem 269:33082-90 (1994)

[hsa:4842]

PMID:7682706

Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR

Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes.

Proc Natl Acad Sci U S A 90:3491-5 (1993)
DOI:10.1073/pnas.90.8.3491

[hsa:4843]

PMID:1378832

Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD

Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase.

J Biol Chem 267:14519-22 (1992)

[hsa:4846]

PMID:19321706

Li JH, Liu YQ, Lu P, Lin HF, Bai Y, Wang XC, Chen YL

A signaling pathway linking nitric oxide production to heterotrimeric G protein and hydrogen peroxide regulates extracellular calmodulin induction of stomatal closure in Arabidopsis.

Plant Physiol 150:114-24 (2009)
DOI:10.1104/pp.109.137067

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

L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)

2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O (overall reaction) [RN:R00557];
(1a) 2 L-arginine + 2 NADPH + 2 H+ + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O  [RN:R00558];
(1b) 2 Nomega-hydroxy-L-arginine + NADPH + H+ + 2 O2 = 2 L-citrulline + 2 nitric oxide + NADP+ + 2 H2O [RN:R00111]

R00111 R00557 R00558
Reaction

L-arginine [CPD:C00062];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007];
Nomega-hydroxy-L-arginine

The enzyme consists of linked oxygenase and reductase domains. The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. cf. EC 1.14.14.47, nitric-oxide synthase (flavodoxin).

EC 1.14.13.39 created 1992, modified 2012, modified 2017