EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.15.1.1 | -999 |
- |
- |
678129 |
| 1.15.1.1 | -999 |
- |
a higher thermostable enzyme |
745093 |
| 1.15.1.1 | -999 |
- |
a highly thermostable enzyme |
745093 |
| 1.15.1.1 | -999 |
- |
a highly thermostable enzyme, occurrence of an additional sulfur-containing hydrogen bond involving the M110 residue and the effect of the A138 residue on the backbone entropy |
745093 |
| 1.15.1.1 | -999 |
- |
a thermostable enzyme |
745093 |
| 1.15.1.1 | -999 |
- |
activation energy for enzyme thermal denaturation, 143.5 kJ per mol |
660283 |
| 1.15.1.1 | -999 |
- |
an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared to the enzyme from Escherichia coli, structure-thermostability relationship, overview |
701534 |
| 1.15.1.1 | -999 |
- |
an increased number of charged residues and an increase in the number of intersubunit salt bridges and the Thr:Ser ratio compared to enzymes from other species are identified as potential reasons for the thermostability of CtMnSOD |
727097 |
| 1.15.1.1 | -999 |
- |
circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD. Thermal inactivation first-order kinetics |
746336 |
| 1.15.1.1 | -999 |
- |
comparison of thermostability of various Gluconobacter strains |
438139 |
