EC Number   |
|---|
   1.14.14.47 | binding of substrate L-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthase from a loose dimer, with an exposed active center and higher sensitivity to proteolysis, to a tight dimer competent for catalysis |
| 1.14.14.47 | enzyme exhibits two conformations in the absence of substrate. The addition of L-Arg stabilizes the conformer more similar to the Mus muculus enzyme, whereas N-hydroxy-L-arginine stabilizes the conformer more similar to the Bacillus subtilis enzyme, although both substrates introduce a positive electrostatic potential to the distal heme pocket |
| 1.14.14.47 | in complex with a number of inhibitors |
| 1.14.14.47 | in complex with cofactor tetrahydrofolate and substrate L-arginine or the intermediate Nomega-hydroxy-L-arginine to 1.9 or 2.2 Å resolution, respectively |
| 1.14.14.47 | in complex with inhibitors that target both the active and pterin sites |
| 1.14.14.47 | incomplex with inhibitors 6-([(3R,5S)-5-][[[[(6-amino-4-methylpyridin-2-yl)methoxy]methyl]pyrrolidin-3-yl]oxy]methyl)-4-methylpyridin-2-amine and 6,6'-[[(2S,3S)-2-aminobutane-1,3-diyl]bis(oxymethanediyl)]bis(4-methylpyridin-2-amine) |
| 1.14.14.47 | structures of the Fe(III)-NO complex with Nomega-hydroxy-L-arginine show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound Nomega-hydroxy-L-arginine. In the Fe(II)-NO complexes, the protonated Nomega-hydroxy-L-arginine Nomega atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. The L-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen |
| 1.14.14.47 | to 2.4 A resolution. Heme and inhibitor S-ethylisothiourea are bound at the active site, while the intersubunit site has NAD+ bound. Enzyme is a dimer, with NAD+ in the interface ligand binding site. Heme is buried in the interior of each monomer |
| 1.14.14.47 | to 3.2 A resolution. Residue Lys-356 (Bacillus subtilis NOS) is changed to Arg-365 (gsNOS), substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme |
| 1.14.14.47 | wild-tye and mutant I208V, in complex with inhibitors |
