EC Number   |
pH Minimum |
pH Maximum |
Reference |
|---|
    4.1.1.15 | -999 |
- |
effect of pH on enzymatic activities of recombinant wild-type and mutant BmGADs, overview |
747386 |
| 4.1.1.15 | -999 |
- |
pH rise caused by the reaction inactivates the enzyme catalyst, which is active only under acidic conditions, and consequently leads to low reaction conversions |
748287 |
| 4.1.1.15 | -999 |
- |
sigmoidal pH-dependence curve. Enzyme BmGadB displays its maximal activity at low pH, but only up to pH 4.5. At pH 5.0 the enzyme exhibits 50% of the activity measured at pH 3.8-4.5 and activity becomes undetectable at a pH higher than pH 5.6. In the range of pH 3.8-5.3 BmGadB is 1.5-3 times more active when chloride ions are present |
747785 |
| 4.1.1.15 | -999 |
- |
the deletion mutant GADDELTAC is more active above pH 5.6. At pH 6.0, the mutant enzyme still retains 12% of its maximum activity while the wild-type enzyme almost loses all its activity. The enzyme deletion mutant GADDELTAC exhibits 4.8fold higher activity at pH 6.0 compared to the wild-type enzyme |
727378 |
| 4.1.1.15 | -999 |
- |
the enzyme significantly loses activity at near-neutral pH |
727389 |
| 4.1.1.15 | 2.5 |
7.5 |
activity range, profile overview |
749272 |
| 4.1.1.15 | 3 |
6 |
activity range, profile overview |
726685 |
| 4.1.1.15 | 3 |
7 |
purified recombinant enzyme, the activity decreases dramatically between pH 5.0 and pH 7.0. GAD-V exhibits a much higher activity than GAD-C below pH 5.0. More than 80% of the maximum catalytic activity is observed for GAD-V between pH 4.0 and pH 5.0, while GAD-C exhibits 98.3% and 38% of the activity shown by GAD-V at pH 5.0 and 4.0, respectively |
749087 |
| 4.1.1.15 | 3 |
9 |
activity range, profile overview |
727569 |
| 4.1.1.15 | 3.3 |
5.8 |
pH 3.3: about 20% of maximal activity, pH 3.5: about 65% of maximal activity, pH 5.2: about 55% of maximal activity, pH 5.8: about 20% of maximal activity |
3994 |
