EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.4.21.111 | -999 |
- |
significance of salt bridges in the thermal stability of the enzyme, overview |
731114 |
| 3.4.21.111 | 70 |
- |
80% activity after 30 min |
650597 |
| 3.4.21.111 | 70 |
- |
P7I mutant is less thermostable than the wild type enzyme and other mutants in the study, complete loss of activity upon 2 h incubation at 70°C, half life: 60 min |
680550 |
| 3.4.21.111 | 70 |
- |
wild type and P240N mutant retain 60% of activity after 2 h incubation at 60°C |
680550 |
| 3.4.21.111 | 70 |
80 |
0-120 min, pH 6.0, different stabilities of wild-type and mutant enzymes at 70-80°C, inactivations, overview. The inactivation mechanism of enzyme mutant D212N at 80°C may be different from that of enzyme mutants D17N and E237Q at 70°C |
731114 |
| 3.4.21.111 | 70 |
80 |
P268T mutant almost as stable as the wild type enzyme |
680550 |
| 3.4.21.111 | 75.7 |
- |
transition temperature of the P7I mutant enzyme |
680550 |
| 3.4.21.111 | 80 |
- |
P5N mutant much more thermolabile than the wild type enzyme, half life at 80°C: 25 min |
680550 |
| 3.4.21.111 | 80 |
- |
P7I mutant is less thermostable than the wild type enzyme and other mutants in the study, half life: 10 min |
680550 |
| 3.4.21.111 | 80 |
- |
rapid inactivation in absence of Ca2+ |
650593 |
