EC Number   |
pH Stability |
pH Stability Maximum |
Reference |
|---|
   1.8.1.8 | 5.5 |
- |
5°C or 22°C, irreversible inactivation |
437710 |
| 1.8.1.8 | 5.8 |
- |
the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0 |
745638 |
| 1.8.1.8 | 7 |
- |
the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0 |
745638 |
| 1.8.1.8 | 10 |
- |
at pH 10.0 the protein undergoes partial unfolding. Decrease in alpha-helix content at pH 10.0, whereas the beta-sheet content remains unaltered. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0. The C terminal active site at 20°C shows a reduced flexibility at all pH values, while at 100°C the flexibility increases with the pH, with a high value at pH 7.0 |
745638 |
