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Literature summary for 3.4.21.B48 extracted from
- Synergetic effects of pressure and chemical denaturant on protein unfolding: stability of a serine-type carboxyl protease, kumamolisin (2006), Biochim. Biophys. Acta, 1764, 364-371.
General Stability
| General Stability | Organism |
|---|---|
| the enzyme is stable against perturbation by pressure and chemical denaturants | Bacillus novosp. |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | thermodynamic analysis | Bacillus novosp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus novosp. | - |
- |
- |
| Bacillus novosp. MN-32 | - |
- |
- |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
- |
Bacillus novosp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermostability analysis, denaturation curve, the enzyme is stable against thermal perturbation, 8 M urea reduces thermal stability of the enzyme, decreased cotton effect at 55°C, overview | Bacillus novosp. |
| 79.4 | - |
denaturation temperature | Bacillus novosp. |
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