EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
---|
3.5.4.27 | -999 |
- |
at cyclic 2,3-diphosphoglycerate concentrations prevailing in the cells of Methanopyrus kandleri the enzyme is completely thermostable. At molar concentrations also the potassium salts of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cyclic 2,3-diphosphoglycerate confer thermostability to the enzymes |
726828 |
3.5.4.27 | -999 |
- |
no requirement of salts for thermostability |
246740 |
3.5.4.27 | -999 |
- |
salts increase heat stability of the enzyme |
209741 |
3.5.4.27 | 60 |
- |
10 min, 50% loss of activity in absence of salts. Stable for 25 min in presence of salt, 1 M K2HPO4 |
209741 |
3.5.4.27 | 60 |
- |
stable up to |
486097 |
3.5.4.27 | 65 |
- |
stable up to |
486097 |
3.5.4.27 | 90 |
- |
- |
246740 |
3.5.4.27 | 90 |
- |
1.5 M K2HPO4 is required for optimal stability |
246740 |
3.5.4.27 | 90 |
- |
60 min, 50 mM tricine/KOH, pH 8, stable |
246741 |
3.5.4.27 | 90 |
- |
enzyme in 40 mM potassium phosphate, pH 8.0, 1 h, 8% activity remaining, with addition of 0.5 M cyclic 2,3-bisphosphoglycerate or 0.7 M bisphosphoglycerate or 1.5 M phosphate, 100% activity are remaining |
755911 |