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1.14.14.47: nitric-oxide synthase (flavodoxin)

This is an abbreviated version!
For detailed information about nitric-oxide synthase (flavodoxin), go to the full flat file.

Word Map on EC 1.14.14.47

Reaction

2 L-arginine + 2 reduced flavodoxin + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O

Synonyms

bNOS, GK1676, nitric oxide synthetase, NO synthase, NOS, SANOS, YumC

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.47 nitric-oxide synthase (flavodoxin)

Crystallization

Crystallization on EC 1.14.14.47 - nitric-oxide synthase (flavodoxin)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
in complex with a number of inhibitors
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
in complex with inhibitors that target both the active and pterin sites
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)
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
wild-tye and mutant I208V, in complex with inhibitors
wild-type in complex with inhibitors N-omega-nitro-L-arginine and 3-bromo-7-nitroindazole
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
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
-
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