EC Number   |
pH Stability |
pH Stability Maximum |
Reference |
|---|
   1.1.3.17 | -999 |
- |
at higher pH a transition from alpha-helix to beta-structure occurs while at lower pH the content of alpha-helix structure increases (circular dichroism). Enzyme is more instable at higher pH (melting temperature decreases). At high alkaline pH values the enzyme reveals more accessible hydrophobic patches relative to acidic pH (fluorescence measurement) |
697063 |
| 1.1.3.17 | -999 |
- |
comparison of pka values of the mutants V464A and V464T |
696243 |
| 1.1.3.17 | -999 |
- |
low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity |
677058 |
| 1.1.3.17 | -999 |
- |
more rapid inactivation at alkaline than at acidic pH at both 27°C and 37°C. pH-dependent secondary structure changes are analysed |
695307 |
| 1.1.3.17 | -999 |
- |
prolonged incubation of the inactive enzyme at pH 6 and temperatures above 20°C reveals slow and full recovery of activity over 3 hours, linked to conformational change reverting the enzyme to the native form, rate of approaching steady state independent of concentrations of choline and enzyme, increased to a limiting value with increasing pH |
689966 |
| 1.1.3.17 | 3 |
6 |
inactivation takes place at both 27°C and 37°C |
695307 |
| 1.1.3.17 | 6 |
9 |
inactivation takes place at both 27°C and 37°C |
695307 |
| 1.1.3.17 | 7 |
8.5 |
no significant inactivation at both 27°C and 37°C |
695307 |
| 1.1.3.17 | 7 |
9 |
50% initial activity is lost at 40°C at pH 6.0 and 9.5 |
389719 |
| 1.1.3.17 | 8 |
10.2 |
purified enzyme, 30°C, 10 min, stable at |
724598 |
