EC Number   |
Inhibitors |
Structure |
|---|
   3.4.21.92 | CAANDENYALAA-NH2 |
- |
   |
| 3.4.21.92 | ClpS |
adaptor protein ClpS is inhibitory to ClpC1. the unfolding rate of substrates shows a a nearly three-fold for conditions lacking ClpS relative to conditions with ClpS in excess |
|
| 3.4.21.92 | cyclomarin |
cyclomarin binding to subunit ClpC1 N-terminal domain specifically blockes the N-terminal dynamics induced by arginine-phosphate binding. Cyclomarin-induced restriction of ClpC1 dynamics may modulate the chaperone enzymatic activity leading eventually to cell death |
|
| 3.4.21.92 | diisopropyl fluorophosphate |
inhibits both oligopeptidase activity of ClpP and proteinase activity of ClpAP |
|
| 3.4.21.92 | diisopropyl fluorophosphate |
inactivates ClpP |
|
| 3.4.21.92 | diisopropyl fluorophosphate |
blocks similarly the hydrolysis of both protein and peptide substrates |
|
| 3.4.21.92 | diisopropyl fluorophosphate |
inhibitor efficiently alters the oligomerization of the enzyme to smaller species, almost quantitative shift from the tetradecamer to the heptamer with modification of 57% of the active sites |
|
| 3.4.21.92 | diisopropylfluorophosphate |
- |
|
| 3.4.21.92 | fluorosulfonylbenzoyladenosine |
- |
|
| 3.4.21.92 | High salt concentrations |
chloride is much more inhibitory than acetate, divalent anions are also very inhibitory |
|
