nitric-oxide synthase (NADPH) EC#: 1.14.13.39; ChemWhat Code: 1375254
| Product Name | nitric-oxide synthase (NADPH) |
| Example Structure |  |
| Synonyms | bacterial nitric oxide synthase, bacterial nitric-oxide synthase, bNOS, bsNOS, cb-NOS, cytokine inducible NOS, DNOS, e-NOS, EC-NOS, endothelial nitric oxide synthase, endothelial nitric-oxide synthase, endothelial NO synthase, endothelial NOS, endothelium-derived relaxation factor-forming enzyme, endothelium-derived relaxing factor synthase, eNOS, i-NOS, inducible nitric oxide synthase, inducible nitric-oxide synthase, inducible NO synthase, inducible NOS, iNOS, mitochondrial NO synthase, mitochondrial-specific nitric oxide synthase, mtNOS, n-NOS, NADPH diaphorase, NADPH-diaphorase, neuronal nitric oxide synthase, neuronal nitric-oxide synthase, neuronal NO synthase, neuronal NOS, nitric oxid synthase, nitric oxide synthase, nitric oxide synthase-like protein, nitric oxide synthetase, nitric-oxide synthase, nNOS, nNOSalpha, NO synthase, NO synthase type I, NO synthase type II, NO synthase type III, NO synthases, NO-synthase, NOS, NOS I, NOS-2, NOS1, NOS2, NOS3, synthetase, nitric oxide |
| EC Number | 1.14.13.39 |
| CAS Registry Number | 125978-95-2 |
| Comments | 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). |
| Cofactor | 5,6,7,8-tetrahydrobiopterin;FMN;FAD;heme |
| History | |
| Reactions | 2 L-arginine + 3 Nadph + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. |
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