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Literature summary for 3.4.21.66 extracted from
- Influence of synthetic peptide inhibitors on the thermal stability of thermitase, a serine proteinase from Thermoactinomyces vulgaris (1984), Int. J. Pept. Protein Res., 23, 134-141.
General Stability
| General Stability | Organism |
|---|---|
| Irreversible inhibition by chloromethyl ketones causes marked stabilization against thermal denaturation, reversible inhibitors have no influence on stability | Thermoactinomyces vulgaris |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Chloromethyl ketones | irreversible | Thermoactinomyces vulgaris |  |
| Methyl ketones of N-acylated peptides | 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 | - |
irreversible inhibition by chloromethyl ketones causes marked stabilization against thermal denaturation | Thermoactinomyces vulgaris |
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