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Literature summary for 3.2.1.6 extracted from
- Study of the influence of temperature on the dynamics of the catalytic cleft in 1,3-1,4-beta-glucanase by molecular dynamics simulations (2006), J. Mol. Model., 12, 835-845.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N207D | increase in Tm-value to 75.3°C, compared to wild-type Tm-value of 71.4°C | Bacillus licheniformis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus licheniformis | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
hypothesis for thermal inactivation: the first phase in thermal denaturation could be produced when calcium interactions are disrupted and the main loop becomes free to rearrange. This phase yields a partially active intermediary during the first phase of inactivation and then the intermediary is slowly converted into a totally inactive enzyme in the second phase | Bacillus licheniformis |
| 71 | - |
Tm-value for wild-type enzyme is 71.4°C | Bacillus licheniformis |
| 75 | - |
Tm-value for mutant enzyme N207D is 75.3°C | Bacillus licheniformis |
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