Related Searches  no synthase  Nitric oxide synthase  Nitric
oxide synthases ()(NOSs) are present among eukaryotic enzymes as
dimeric, calmodulin-dependent or calmodulin-containing
cytochrome p450-like hemoprotein that combine reductase and
oxygenase catalytic domains in one monomer, bear both flavin
adenine dinucleotide (FAD) and flavin mononucleotide (FMN), and
carry out a 5`-electron oxidation of non-aromatic amino acid
L-arginine with the aid of tetrahydro-biopterin. . NOS is an
enzyme in the body that contributes to transmission from one
neuron to another, to the immune system and to dilating blood
vessels. It does so by synthesis of nitric oxide (NO) from the
terminal nitrogen atom of L-arginine in the presence of NADPH
and dioxygen (O2). NOS is the only known enzyme that binds
flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN),
heme, tetrahydrobiopterin (BH4) and calmodulin.  NO activates
Guanylate cyclase, which induces smooth muscle relaxation by:
• increased intracellular cGMP, which