EC Number   |
pH Minimum |
pH Maximum |
Reference |
|---|
   2.3.2.13 | -999 |
- |
the transamidation reaction is kinetically favored over deamidation at pH-values above 7, but the deamidation reaction becomes kinetically competitive as the pH is lowered below 7 or as the concentration of amine substrates is lowered below their Km values |
689380 |
| 2.3.2.13 | 2 |
10 |
activity range, low activity at pH 2.0, high activity at pH 7.4-8.5, maximal activity at pH 8.5, 60% of maximal activity at pH 10.0, profile overview |
759209 |
| 2.3.2.13 | 4 |
9 |
activity range, wild-type and mutant enzyme, profiles overview |
758740 |
| 2.3.2.13 | 4 |
10 |
activity range |
758664 |
| 2.3.2.13 | 5 |
7 |
- |
659617 |
| 2.3.2.13 | 5 |
8 |
activity range of isozyme MTG-TX |
759632 |
| 2.3.2.13 | 5 |
8 |
pH 5.0: about 80% of maximal activity, pH 8.0: about 80% of maximal activity |
686843 |
| 2.3.2.13 | 6 |
9 |
80-100% of maximal activity within this range |
759212 |
| 2.3.2.13 | 6 |
10 |
activity range at 16°C, recombinant enzyme |
759197 |
| 2.3.2.13 | 6.5 |
10 |
pH 6.5: about 65% of maximal activity, pH 10.0: about 60% of maximal activity |
688114 |
