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Literature summary for 1.4.1.2 extracted from
- Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis (1995), Eur. J. Biochem., 229, 688-695 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| [Clostridium] symbiosum | P24295 | - |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 52 | - |
23 min, 56% loss of activity. alignment of the sequences for the thermophilic glutamate dehydrogenases from Thermococcus litoralis and Pyrococcus furiosus against the sequence and the molecular structure of the glutamate dehydrogenase from the mesophile Clostridium symbiosum provides insights into the molecular basis of their thermostability. A relatively small number of amino acid substitutions is observed between the two thermophilic glutamate dehydrogenase sequences. The most frequent amino acid exchanges involves substitutions which increase the hydrophobicity and sidechain branching in the more thermostable enzyme. Particularly common is the substitution of valine to isoleucine. Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures. One hot spot for the accumulation of exchanges lies close to a region of the molecule involved in its conformational flexibility and these changes may modulate the dynamics of this enzyme and thereby contribute to increased stability | [Clostridium] symbiosum |
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