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Literature summary for 3.4.21.64 extracted from
- Thermitase and proteinase K: a comparison of the refined three-dimensional structures of the native enzymes (1990), Protein Eng., 3, 161-172.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| three-dimensional structure at 1.48 A resolution | Parengyodontium album |
General Stability
| General Stability | Organism |
|---|---|
| Relatively stable towards heat and denaturing agents | Parengyodontium album |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Calcium | required for folding of the polypeptide chain | Parengyodontium album |  |
| Calcium | the second more mobile Ca2+ site bridges 2 loops close to the amino and the carboxy termini | Parengyodontium album | |
| Calcium | 2 calcium ions are bound to the native enzyme, activity drops by 70% if this Ca2+ is removed by EDTA | Parengyodontium album | |
| Calcium | the first calcium site is formed by the loop of the residues 174-178 and Asp200 | Parengyodontium album | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Parengyodontium album | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
Ca2+ contributes to the overal stability of the surface regions and improves the thermal stability | Parengyodontium album |
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Release 2023.1 (January 2023)
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