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Literature summary for 3.4.21.81 extracted from
- Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases (2005), J. Mol. Biol., 347, 355-366.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces griseus | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| study of temperature-dependencies of the folding and unfolding kinetics without enzyme pro region. Enzyme shows a maximal unfolding cooperativity and slow rate of global unfolding | Streptomyces griseus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
study of temperature-dependences of the folding and unfolding kinetics without enzyme pro region | Streptomyces griseus |
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Release 2023.1 (January 2023)
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