EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.5.1.3 | -999 |
- |
1 mM NADPH protects against inactivation |
392270 |
| 1.5.1.3 | -999 |
- |
7,8-dihydrofolate protects against heat inactivation |
392245 |
| 1.5.1.3 | -999 |
- |
glycerol and 2-mercaptoethanol shift the midpoint of the thermal transition upwards by about 25°C |
655861 |
| 1.5.1.3 | -999 |
- |
heat stable |
392250 |
| 1.5.1.3 | -999 |
- |
molecular reasons for the high intrinsic stability of the enzyme: the molecule is extremely rigid, even with respect to structural changes during substrate binding and turnover. Major contributions to the high intrinsic stability of the enzyme result from the formation of the dimer. Within the monomer, only subtle stabilizing interactions are detectable. The docking of the subunits is optimized with respect to high packing density in the dimer interface, additional salt-bridges and beta-sheets |
748389 |
| 1.5.1.3 | -999 |
- |
the free energy of stabilization of monomeric mutant enzyme V11D is 15 kJ/mol lower than that of the wild-type dimer, while the melting temperature of monomeric mutant enzyme V11D is comparable to that of monomeric DHFR from the thermophile Bacillus stearothermophilus, supporting the hypothesis that oligomerization is required to achieve the thermal stabilities necessary for activity at temperatures optimal for growth of hyperthermophiles |
747064 |
| 1.5.1.3 | 0 |
- |
cold denaturation below |
655861 |
| 1.5.1.3 | 4 |
- |
above, for extended length of time, unstable |
392267 |
| 1.5.1.3 | 30 |
60 |
when temperature is higher than 30°C, the enzyme activity is decreased rapidly but the comparatively lower velocity is maintained till 60°C |
725924 |
| 1.5.1.3 | 35 |
- |
15 min, stable |
655861 |
