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Literature summary for 3.5.1.11 extracted from
- Thermodynamic and kinetic stability of penicillin acylase from Escherichia coli (2008), Biochim. Biophys. Acta, 1784, 736-746.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
denaturation temperature at pH 3.0 or 9.5 | Escherichia coli |
| 65 | - |
denaturation temperature at pH 6.0 | Escherichia coli |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 9.5 | the enzyme maintains the folded structure in the pH range from pH 3.0 to 9.5 | Escherichia coli |
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