EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    2.7.2.3 | -999 |
- |
- |
642252 |
| 2.7.2.3 | -999 |
- |
decreased thermostability, cold-adapted organism |
642302 |
| 2.7.2.3 | -999 |
- |
L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation |
684894 |
| 2.7.2.3 | -999 |
- |
PGK1 is more heat-stable than PGK2 |
642235 |
| 2.7.2.3 | -999 |
- |
stabilizing effects of anions on thermal stability |
642281 |
| 2.7.2.3 | -999 |
- |
the psychrophilic enzyme enzyme exhibits two distinct stability domains in the free, open conformation. These stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain |
662433 |
| 2.7.2.3 | -999 |
- |
the recombinant His-tagged wild-type enzyme shows reduced thermostability compared to the native and recombinant wild-type without tag |
642296 |
| 2.7.2.3 | -999 |
- |
thermal analysis |
642252, 642287 |
| 2.7.2.3 | -999 |
- |
thermal denaturation at pH 5.5 and pH 7.5 of the isoenzymes |
642267 |
| 2.7.2.3 | 24 |
- |
two stable, folded conformers with an abrupt conformational transition occurring at 24°C. The transition state thermodynamics for the low- to high-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mol and the transition state possesses a significant unfolding quality |
684730 |
