EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
---|
5.3.1.1 | -999 |
- |
crystal structure represents the most thermostable triosephosphate isomerase presently known in its 3D-structure |
653844 |
5.3.1.1 | -999 |
- |
denaturation of the enzyme likely consists of an initial first-order reaction that forms thermally unfolded enzyme, followed by irreversibility-inducing reactions which are probably linked to aggregation of the unfolded protein |
650088 |
5.3.1.1 | -999 |
- |
dimeric enzyme unfolds following a four state model denaturation process whereas monomeric variants follow a three state model |
749068 |
5.3.1.1 | -999 |
- |
Lys13 plays a crucial role in the functional adaptation of the thermophilic enzyme to high temperatures |
651930 |
5.3.1.1 | -999 |
- |
slow temperature-induced unfolding of yeast TIM shows three kinetic phases. A complex mechanism involving off-pathway intermediates or parallel pathways may be operating. beta-Strand-type residual structure appears below pH 8.0, and is likely to be associated with increased irreversible aggregation of the unfolded protein, which accelerates the refolding process |
747403 |
5.3.1.1 | -999 |
- |
the enzyme lacks an intricate network of 4 ion pairs in its 4th beta/alpha unit, (beta/alpha)4. Iintroduction of a thermophile-sourced ion pair network in the fourth beta/alpha unit of a psychophile-derived triosephosphate isomerase from Methanococcoides burtonii significantly increases its kinetic thermal stability. The enzyme with the incorporated ion pair network, shows significantly higher apparent Tm values and also displays significantly higher kinetic thermal stability |
744384 |
5.3.1.1 | -999 |
- |
Thermal melting of PfuTIM in buffers of different pH, overview |
702458 |
5.3.1.1 | 10 |
- |
half-life of wild-type enzyme: 58 min |
2586 |
5.3.1.1 | 22 |
- |
pH 7, stable indefinitely |
2558 |
5.3.1.1 | 25 |
- |
half-life of wild-type enzyme: 10 min, half-life of mutant enzyme A238S: 27 min |
2586 |