EC Number   |
pH Minimum |
pH Maximum |
Reference |
|---|
   1.17.3.2 | -999 |
- |
comparison of the pH dependence of both kred and kred/Kd from reductive half-reaction experiments between wild-type enzyme and mutant E232Q, overview. The ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pKa of the substrate by two pH units and ensuring that at physiological pH the neutral form of the substrate predominates in the Michaelis complex |
745314 |
| 1.17.3.2 | 5 |
9 |
pH 5.0: about 10% of activity maximum, pH 9.0: about 25% of activity maximum |
644623 |
| 1.17.3.2 | 6 |
7.6 |
under aerobic conditions, NO generation increases more than three times as the pH value decreases from pH 7.4 to 6.0 |
659326 |
| 1.17.3.2 | 6 |
9 |
- |
702182 |
| 1.17.3.2 | 6 |
9 |
pH 6.0: about 25% of activity maximum, pH 9.0: about 20% of activity maximum |
644620 |
| 1.17.3.2 | 6.5 |
9.5 |
pH 6.5: about 40% of maximal activity, pH 9.5: about 65% of maximal activity, conversion of dibromoacetonitrile to CN- |
657700 |
| 1.17.3.2 | 6.6 |
8 |
- |
706259 |
| 1.17.3.2 | 7.5 |
9.5 |
potassium phosphate, Tris-HCl, Tris-acetate and glycine-NaOH buffer |
727706 |
| 1.17.3.2 | 7.7 |
9.1 |
at pH 7.7 and 9.1: about 30% of activity maximum |
644639 |
