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Literature summary for 3.1.1.1 extracted from
- Structural study of carboxylesterase from hyperthermophilic bacteria Geobacillus stearothermophilus by molecular dynamics simulation (2010), J. Mol. Graph. Model., 28, 820-827.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | D232-K211, E105-K82, E54-K134, E238-R12 and E147-K134 are critical ion-pairs of fundamental importance in maintaining the structural integrity of the protein structure. Among these five pairs, one ion-pair (D232-K211) is extremely stable throughout the simulation up to 70°C. D232-K211 ion-pair between alphaF and beta8 adds more stability towards thermostable beta-sheet core region | Geobacillus stearothermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Geobacillus stearothermophilus | Q06174 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EST | - |
Geobacillus stearothermophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 27 | 100 | at 27°C, 70°C, and 100°C the enzyme is stable and maintains its global three-dimensional structure | Geobacillus stearothermophilus |
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Release 2023.1 (January 2023)
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