EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    2.4.2.8 | -999 |
- |
- |
638400, 661691 |
| 2.4.2.8 | 30 |
- |
pH 7.4, stable |
638393 |
| 2.4.2.8 | 40 |
- |
pH 7.4, gradual decrease of activity |
638393 |
| 2.4.2.8 | 40 |
45 |
purified recombinant ZgHGPRT/AMPK exhibits an apparent unfolding temperature (Tm) of 45°C and a retained activity of around 80% when incubated at 40°C for 240 min |
759221 |
| 2.4.2.8 | 50 |
- |
half-life: 75 min, irreversible inactivation |
663292 |
| 2.4.2.8 | 60 |
- |
1.5 mM GMP, 10 min, complete loss of activity |
638161 |
| 2.4.2.8 | 60 |
- |
3 h, wild-type and mutant F36L, over 80% remaining activity |
660798 |
| 2.4.2.8 | 60 |
- |
analysis of the stability of the variants in temperature unfolding experiments. Protein aggregation is taking place after dialysis or denaturant dilution, an indication of the existence of an irreversible phenomenon, precludes the derivation of thermodynamic state functions from the unfolding data. But the enzyme behave as cooperative folding units when submitted to thermal denaturation. In particular, a qualitative comparison (a shift in the observed apparent Tm values) of thermal denaturation curves suggests that the His-tag present in TcHPRTH6 might enhance its thermostability by increasing the height of the activation barrier to the formation of aggregation-prone species. Nevertheless, when the enzyme is incubated for 10 min at 60°C, it irreversibly aggregates with a concomitant loss of enzymatic activity |
758845 |
| 2.4.2.8 | 60 |
- |
mutant and wild-type enzyme, 8 min, stable |
638421 |
| 2.4.2.8 | 60 |
65 |
stable |
638358 |
