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Results 1 - 10 of 14 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47E25A/E26A/E316A mutant facilitates crystallization -, 740066
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47E25A/E26A/E316A/Y357F mutant facilitates crystallization -, 740066
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47I208V crystallization and inhibition data -, 740084
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47L356R 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47more 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47more 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47P332G mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type -, 740863
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47P332G/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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47W66F 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.47W66F mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates -, 740692
Results 1 - 10 of 14 > >>