EC Number   |
Protein Variants |
Reference |
|---|
  1.6.3.4 | C42A |
produces H2O2, 90% loss of NADH oxidase activity |
-, 722139 |
| 1.6.3.4 | C44A |
80% of wild-type activity, production of H2O2 rather than H2O |
721809 |
| 1.6.3.4 | D170R |
18.8% loss of activity |
764367 |
| 1.6.3.4 | D219R |
37.6% loss of activity |
764367 |
| 1.6.3.4 | D247R |
60.4% loss of activity |
764367 |
| 1.6.3.4 | D251R |
mutation improves the activity to 112%, 111%, and 244% of the wild-type at pH 6.5, pH 7.0, and pH 7.5, respectively. NADH has access to the substrate-binding site with a larger substrate loop due to the enhanced electrostatic repulsion between Arg251 and Arg243. In the D251R-NADH complex, the carboxyl of NADH additionally forms two hydrogen bonds with G154 due to the changed interaction of substrate and the residues in the catalytic sites, and the hydrogen bond with the oxygen of carbonyl in P295 is shortened from 2.9 to 2.0 A |
764367 |
| 1.6.3.4 | D292A |
mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity |
721809 |
| 1.6.3.4 | D359R |
91% loss of activity |
764367 |
| 1.6.3.4 | E316R |
91% loss of activity |
764367 |
| 1.6.3.4 | G13A |
mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity |
721809 |
