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Literature summary for 3.4.21.B57 extracted from
- Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakaraensis (2010), Biochim. Biophys. Acta, 1814, 299-307.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Thermococcus kodakaraensis serpin | irreversibly inhibits more strongly at 80°C than at 40°C. The covalent inhibitory complex is highly stable and the ester bond between serpin and protease can be hydrolyzed only in a harsh condition, in which most proteases are denatured | Thermococcus kodakarensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | P58502 | sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106) | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Tk-subtilisin | - |
Thermococcus kodakarensis |
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Release 2023.1 (January 2023)
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