EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    2.2.1.1 | -999 |
- |
10% non-cooperative loss of secondary structure as the temperature increases from 5°C to 50°C. This partial unfolding at moderately elevated temperatures may belinked to the enzyme activation observed at up to 55°C prior to the activity loss at higher temperatures. At 40-55°C the residual activity increases with incubation time and temperature when measured after re-cooling samples to 25°C, indicating that the protein undergoes an irreversible annealing, such that inactive forms of the enzyme are physically altered or activated by temperature |
720083 |
| 2.2.1.1 | -999 |
- |
albumin enhances thermal stability |
486006 |
| 2.2.1.1 | -999 |
- |
the enzyme is more stable in presence of Ca2+ than Mg2+. Thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium |
675747 |
| 2.2.1.1 | -999 |
- |
thiamine diphosphate enhances thermal stability |
486002 |
| 2.2.1.1 | 20 |
- |
at pH 6.5-8.7, 20 min stable |
486002, 486003 |
| 2.2.1.1 | 40 |
- |
pH 8.0, activity hardly changes for 60 min |
486002, 486003 |
| 2.2.1.1 | 50 |
- |
1 h stable in the presence of 4 mM thiamine diphosphate |
486003 |
| 2.2.1.1 | 50 |
- |
t1/2: 10 min |
486002, 486003 |
| 2.2.1.1 | 50 |
- |
the enzyme isoforms TKTc and TKTp remain stable up to 50°C for at least 2 h. Upon pre-incubation at 60°C the catalytic activity is reduced for both enzymes to approximately 60% within 10 min and then remains stable at this level. Incubation at 70°C leads to a complete loss of activity for TKTc after 4 min, for TKTp after 30 min of incubation |
735856 |
| 2.2.1.1 | 50 |
85 |
the enzyme shows a half-life of 35 min at 50°C, 15 min at 75°C, and is immediately inactivated at 85°C |
735415 |
