EC Number   |
Protein Variants |
Reference |
|---|
   1.7.1.6 | A123F |
36% of wild-type activity |
724120 |
| 1.7.1.6 | D184G |
complete loss of activity |
724120 |
| 1.7.1.6 | E16G |
46% of wild-type activity |
724120 |
| 1.7.1.6 | F127G |
complete loss of activity |
724120 |
| 1.7.1.6 | F162A |
Phe-162 is chosen because it is predicted to participate in the substrate binding on top of the isoalloxazine ring, as observed in the AzoR-inhibitor structure |
698751 |
| 1.7.1.6 | H75N |
mutation decreases the binding of methyl red and nitrofurazone and has no effect on the bining of NADPH |
696902 |
| 1.7.1.6 | K109A |
K109 might only be involved in the binding of the 2'-phosphate group of NADPH and have no effect on the binding of NADH |
696902 |
| 1.7.1.6 | K109H |
K109 might only be involved in the binding of the 2'-phosphate group of NADPH and have no effect on the binding of NADH |
696902 |
| 1.7.1.6 | L49C/D108C |
the mutant enzyme shows increased thermal stability at 50°C (increased half-life from 12.6 min in wild type to 26.66 min in the mutant enzyme). The mutant enzyme can also tolerate 5% (w/v) NaCl and retains 30% of original activity after 24 h incubation |
764338 |
| 1.7.1.6 | L59G |
10% of wild-type activity |
724120 |
