EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    3.1.3.11 | -999 |
- |
AMP and fructose 1,6-diphosphate increase thermal stability |
170759 |
| 3.1.3.11 | -999 |
- |
AMP binding results in improved thermal stability of muscle FBPase |
749494 |
| 3.1.3.11 | -999 |
- |
fructose 1,6-diphosphate, Mg2+ and Mn2+ protect against thermal inactivation |
170763 |
| 3.1.3.11 | -999 |
- |
the archaeal FBP aldolase/phosphatases are highly thermostable |
705891 |
| 3.1.3.11 | 0 |
50 |
the recombinant enzyme is stable |
653727 |
| 3.1.3.11 | 4 |
- |
purification at 4°C, loss of 80% of the enzyme activity |
666587 |
| 3.1.3.11 | 8 |
56.5 |
temperature midpoint for the protein unfolding transition of enzyme LmFBPase is 56.5°C, thermostability in the presence of the substrate fructose-2,6-bisphosphate is highly increased for LmFBPase with a DELTATm of about 8°C. The stabilization effect of the substrate is not eliminated by AMP, but the stabilizing effects are additive. Thermostability of LmFBPase is increased by more than 9°C in the presence of Mn2+ |
751333 |
| 3.1.3.11 | 10 |
30 |
purified recombinant His-tagged enzyme, 30 min, completely stable |
713798 |
| 3.1.3.11 | 30 |
- |
half-life: 1 h, enzyme from methanol-grown cells |
170732 |
| 3.1.3.11 | 37 |
- |
half-life: 5 min, enzyme from methanol-grown cells |
170732 |
