Three NOS isozymes are found in animals: neuronal NOS, endothelial NOS, and inducible NOS.
Although they differ when it comes to amino acid sequence (51-57% homology), they all share similar structures. They are homodimeric with each monomer containing a N-terminal oxygenase domain and a C-terminal reductase domain. The N-terminal oxygenase domain contains binding sites for the catalytic heme, tetrahydrobiopterin (H4B), and the substrates L-arginine and molecular oxygen. The C-terminal domain contains binding sites for cofactors FMN, FAD, and NADPH. A calmodulin binding domain connects the two domains in each monomer.
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