Literature summary for 3.4.22.14 extracted from

Grozdanovic, M.M.; Drakulic, B.J.; Gavrovic-Jankulovic, M.
Conformational mobility of active and E-64-inhibited actinidin (2013), Biochim. Biophys. Acta, 1830, 4790-4799.

Inhibitors

Inhibitors	Comment	Organism	Structure
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide	conformational mobility of actinidin changes upon binding of the inhibitor E-64, leading to a sequence of events that enables water and ions to protrude into a newly formed cavity of the inhibited enzyme	Actinidia deliciosa

Organism	UniProt	Comment	Textmining
Actinidia deliciosa	-	-	-

Synonyms	Comment	Organism
actinidin	-	Actinidia deliciosa

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Release 2023.1 (January 2023)