EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   2.7.7.7 | -999 |
- |
DNA polymerase Dpo2 and Dpo3 are more thermolabile than Dpo1 and Dpo4 |
725439 |
| 2.7.7.7 | -999 |
- |
heat stability of polymerase I, II and III |
643598 |
| 2.7.7.7 | -999 |
- |
the (G)-PYF box motif mediates intersubunit interactions, which may be crucial for the thermostability of the enzyme |
722960 |
| 2.7.7.7 | -999 |
- |
the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 100°C |
724944 |
| 2.7.7.7 | -999 |
- |
the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 107.5°C |
724944 |
| 2.7.7.7 | -999 |
- |
the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 111°C |
724944 |
| 2.7.7.7 | -999 |
- |
the enzyme shows higher thermostability |
723030 |
| 2.7.7.7 | -999 |
- |
wild-type enzyme exhibits a three-state cooperative unfolding profile, with an unfolding intermediate existing between the native and denatured states. The native state of wild-type Dpo4 persists from 26 to 87.5°C, and the unfolding intermediate is observed between 92 and 96.5 °C. Starting at 110 °C, the molar ellipticity approaches its highest value and does not change significantly in the temperature range of 110°C to 119°C. The Little Finger domain of the enzyme, which is only found in the Y-family DNA polymerases, is more thermostable than the polymerase core. The enzyme exhibits a three-state cooperative unfolding profile with an unfolding intermediate. The linker region between the Little Finger and Thumb domains of Dpo4 is a source of structural instability. Through site-directed mutagenesis, the interactions between the residues in the linker region and the Palm domain are identified to play a critical role in the formation of the unfolding intermediate. The secondary structure of Dpo4 is not altered when the temperature is increased from 26 to 87.5°C |
724743 |
| 2.7.7.7 | 25 |
- |
stable for 3 h in an optimized reaction buffer |
661096 |
| 2.7.7.7 | 25 |
95 |
thermostability and half-life of the LF Bst polymerase with the attached TopoV's HhH C2 domain increases almost 8fold, as compared to the Bst LF polymerase alone. The effect can be seen up to 95°C. The stabilizing effect of the C3 domain in N-TopoTaq completely disappears if K-Glu is replaced by 0.5 M NaCl, and the stability of N-TopoTaq does not differ from that of the catalytic domain alone, addition of 1 M betaine restores the stabilization provided by the C3 domain. Electrostatic enhancement of diffusion-controlled association. Thermal stabilization of chimeric polymerases occurs due to charge-independant interactions of the polymerase domain and HhH domains |
721660 |
