EC Number |
Protein Variants |
Reference |
---|
1.7.3.1 | C397S |
the mutant shows reduced activity compared to the wild type enzyme |
764012 |
1.7.3.1 | C397S |
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme |
711373 |
1.7.3.1 | D399N |
the mutation decreases the kcat/KM value for nitroethane over 2 orders of magnitude |
711248 |
1.7.3.1 | D402A |
site-directed mutation of the active site base, 20fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme |
655786 |
1.7.3.1 | D402E |
mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme, determined at 2.4 A resolution, shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402. The interaction of this residue with Ser276 is perturbed |
685114 |
1.7.3.1 | D402E |
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, mutation has no effect on the rate of reaction of the reduced enzyme with oxygen, reaction mechanism analysis |
654710 |
1.7.3.1 | D402E |
the mutant shows severely reduced activity compared to the wild type enzyme |
764012 |
1.7.3.1 | D402E |
the mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402 (compared to mutant enzyme R409K), and the interaction of this residue with Ser276 is perturbed |
685114 |
1.7.3.1 | D402N |
no detectable activity with neutral substrates. Crystallization data in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD |
696325 |
1.7.3.1 | D402N |
site-directed mutation of the active site base, 140fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme |
655786 |