EC Number |
Protein Variants |
Reference |
---|
1.14.14.47 | E25A/E26A/E316A |
mutant facilitates crystallization |
-, 740066 |
1.14.14.47 | E25A/E26A/E316A/Y357F |
mutant facilitates crystallization |
-, 740066 |
1.14.14.47 | I208V |
crystallization and inhibition data |
-, 740084 |
1.14.14.47 | L356R |
mutation Lys-356 (Bacillus subtilis NOS) to Arg-365 (gsNOS) substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme |
740683 |
1.14.14.47 | more |
a chimera between enzyme and flavodoxin YkuN is 8fold more active tan wild-type. Adding excess amounts of YkuN does not significantly alter activity |
-, 740728 |
1.14.14.47 | more |
the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. A fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions |
-, 740692 |
1.14.14.47 | P332G |
mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type |
-, 740863 |
1.14.14.47 | P332G/A333S |
mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme |
-, 740863 |
1.14.14.47 | W66F |
mutation changes midpoint potential from -361 mV for wild-type to -427 mV. Mutant displays 2.5fold lower activity when reaction is supported by flavoproteins or NADPH instead of tetrahydrofolate |
719983 |
1.14.14.47 | W66F |
mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates |
-, 740692 |