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Literature summary extracted from
- Conformational mobility of active and E-64-inhibited actinidin (2013), Biochim. Biophys. Acta, 1830, 4790-4799.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.22.14 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.14 | Actinidia deliciosa | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.22.14 | actinidin | - |
Actinidia deliciosa |
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Release 2023.1 (January 2023)
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