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

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Release 2023.1 (January 2023)