Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH, and oxygen) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin, and heme). Several distinct NOS isoforms are produced from three distinct genes, inducible NOS (iNOS, NOS-II), neuronal NOS (bNOS, NOS-I), and endothelial NOS (eNOS, ecNOS, NOS-III). The inducible form of NOS, iNOS, is Ca2+ independent and is expressed in a broad range of cell types in response to stimulation with cytokines and exposure to microbial products. Phosphorylation of iNOS may regulate its activity and stability. Src kinase-induced phosphorylation of Tyr-1055 in iNOS reduces proteasomal degradation of iNOS leading to increased NO production. Thus, phosphorylation may be an additional control for regulating iNOS activity in response to inflammatory conditions.
Tyryshkin, A. et al. (2009) J Biol Chem. 285(1):784.
Kleinert, H. et al. (2003) Biol Chem. 384(10-11):1343.
Xie, Q.W. et al. (1992) Science 256:225.
*For more information, see UniProt Accession P35228
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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