Literature summary extracted from
Tanaka, S.; Koga, Y.; Takano, K.; Kanaya, S.
Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakaraensis (2010), Biochim. Biophys. Acta, 1814, 299-307.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.4.21.B57 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.B57 |
Thermococcus kodakarensis |
P58502 |
sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106) |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.21.B57 |
Tk-subtilisin |
- |
Thermococcus kodakarensis |