Abstract
The predicted amino acid sequences for nitric oxide synthases (NOSs) contain numerous consensus binding sites for regulatory cofactors, while the genomic structure reveals complex gene promoters and alternate splicing forms. The amino acid sequence of murine macNOS is approximately 50% identical to both bNOS and eNOS. The protein kinase A phosphorylation site conserved between brain NOS (bNOS) and endothelial NOS (eNOS) is absent. NOS catalyzes a five electron oxidation of one of the two equivalent amidine groups of L-arginine to form NO and L-citrulline. The odd electron stoichiometry of the reaction is highly unusual and allows for the generation of the free radical, NO. NOS enzymes can be discriminated by their dependence on calcium. In the brain, calcium influx through glutamate receptor channels or voltage-activated calcium channels stimulates calmodulin, thereby activating NOS. This mode of activation explains the ability of glutamate or neuronal depolarization to stimulate NO formation in a matter of seconds. NOS is also transiently expressed in embryonic sensory neurons, including cells of the dorsal root, trigeminal, nodose, and jugular ganglia.
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