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Literature summary for 3.4.21.66 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 |
|---|---|
| comparison of the refined three-dimensional structure | Thermoactinomyces vulgaris |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | three calcium binding sites, two of these are tight binding sites, and removal of calcium causes unfolding and autolysis to occur. The third calcium is more weakly bound, its removal reduces the activity of the enzyme by 10%, the reduction being reversible | Thermoactinomyces vulgaris |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoactinomyces vulgaris | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
calcium ions contribute to the overall stability of the surface regions and improve the thermal stability of the enzyme | Thermoactinomyces vulgaris |
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Release 2023.1 (January 2023)
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