EC Number   |
Inhibitors |
Structure |
|---|
   3.4.22.14 | Mg2+ |
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition |
   |
| 3.4.22.14 | Mn2+ |
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition |
|
| 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 |
|
| 3.4.22.14 | N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide |
in contrast to actinidin without inhibitor, the actinidinE-64 complex starts degrading 15 min after incubation in simulated gastric fluid (SGF) and is fully degraded after 60 min of incubation. In addition transition maximum temperature (Tm) of the actinidin-inhibitor complex is 61°C in contrast to Tm: 73.9° of actinidin without inhibitor |
|
| 3.4.22.14 | N-acetyl-L-Arg |
- |
|
| 3.4.22.14 | N-benzoyl-L-Arg |
- |
|
| 3.4.22.14 | N-benzoyl-L-Arg ethyl ester |
- |
|
| 3.4.22.14 | NaCl |
minimal activity at 0.5-1.2 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.2 M |
|
| 3.4.22.14 | PCMB |
- |
|
| 3.4.22.14 | Zn2+ |
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition |
|
