3.4.21.92 (4R)-3-(4-methoxyphenyl)-4-(pent-4-yn-1-yl)oxetan-2-one inhibitor efficiently alters the oligomerization of the enzyme to smaller species, almost quantitative shift from the tetradecamer to the heptamer with modification of 35% of the active sites 199410 3.4.21.92 1-(1,1-dioxido-1,2-thiazetidin-2-yl)hexan-1-one alkyne-free beta-sultam analogue. Treatment leads to dehydroalanine formation of the active site serine. The reaction proceeds through sulfonylation and subsequent elimination, thereby obliterating the catalytic charge relay system 199414 3.4.21.92 1-(4-benzoyl-1,1-dioxido-1,2-thiazetidin-2-yl)ethanone alkyne-free beta-sultam analogue. Treatment leads to dehydroalanine formation of the active site serine. The reaction proceeds through sulfonylation and subsequent elimination, thereby obliterating the catalytic charge relay system 199412 3.4.21.92 1-[4-(4-ethynylbenzoyl)-1,1-dioxido-1,2-thiazetidin-2-yl]ethanone treatment results in almost instant covalent modification of all 14 active sites and complete inhibition of peptidase activity 199411 3.4.21.92 1-[4-(4-ethynylbenzoyl)-1,1-dioxido-1,2-thiazetidin-2-yl]undec-10-en-1-one inhibitor efficiently alters the oligomerization of the enzyme to smaller species, almost quantitative shift from the tetradecamer to the heptamer with modification of 63% of the active sites 199409 3.4.21.92 1-[4-benzoyl-1,1-dioxido-1,2-thiazetidin-2-yl]undec-10-en-1-one alkyne-free beta-sultam analogue. Treatment leads to dehydroalanine formation of the active site serine. The reaction proceeds through sulfonylation and subsequent elimination, thereby obliterating the catalytic charge relay system 199413 3.4.21.92 3-(4-methoxyphenyl)-4-(pent-4-ynyl)oxetan-2-one shows stronger inhibitory effect 73175 3.4.21.92 3-(non-8-ynyl)-4-(pent-4-ynyl)oxetan-2-one exerts the weakest effect on peptidase activity 73181 3.4.21.92 3-butyl-4-(pent-4-ynyl)oxetan-2-one shows stronger inhibitory effect 73190 3.4.21.92 CAANDENYALAA - 141886 3.4.21.92 CAANDENYALAA-NH2 - 141887 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 239744 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 239745 3.4.21.92 diisopropyl fluorophosphate inhibits both oligopeptidase activity of ClpP and proteinase activity of ClpAP 244 3.4.21.92 diisopropyl fluorophosphate inactivates ClpP 244 3.4.21.92 diisopropyl fluorophosphate blocks similarly the hydrolysis of both protein and peptide substrates 244 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 244 3.4.21.92 diisopropylfluorophosphate - 299 3.4.21.92 fluorosulfonylbenzoyladenosine - 96505 3.4.21.92 High salt concentrations chloride is much more inhibitory than acetate, divalent anions are also very inhibitory 31222 3.4.21.92 kappa-casein strong, competitive 4316 3.4.21.92 Mg2+ proteolytic activity of ClpAP is dependent on, but concentrations higher than about 30 mM are inhibitory 6 3.4.21.92 additional information ClpP of E. coli has a serine and a histidine that are necessary for activity and probably represent two elements of the active site triad found in most serine proteases 2 3.4.21.92 additional information anti-infection activity and production of hyperimmune antibodies induced by mucosal immunization with ClpP and CbpA can be abrogated by the depletion of CD4+ T lymphocytes. Hyperimmune mouse sera against ClpP and CbpA can inhibit pneumococcus adhesion to cultured A549 epithelial cells and are efficiently opsonic for uptake and killing of pneumococcus by human polymorphonuclear leukocytes in a complement-dependent assay 2 3.4.21.92 additional information not inhibitory: 4-(2-aminoethyl) benzenesulfonyl fluoride, phenylmethylsulfonyl fluoride as well as Z-L-CMK and N-p-tosylphenylalanyl chloromethyl ketone 2 3.4.21.92 NEM - 89 3.4.21.92 NEM inactivates ATPase, no inhibition of peptide hydrolysis 89 3.4.21.92 Neohydrin - 94480 3.4.21.92 phosphoarginine - 94766 3.4.21.92 rufomycin I cyclic peptide with potent and selective in vitro activity against Mycobacterium tuberculosis and Mycobacterium abscessus. Compound significantly decreases the proteolytic capabilities of the ClpC1/P1/P2 complex to degrade casein, while having no significant effect on the ATPase activity of ClpC1 234959 3.4.21.92 Succinyl-Leu-Tyr 4-methylcoumarin 7-amide at high concentrations complete inhibition of casein breakdown 15972 3.4.21.92 Xaa-Tyr-Leu-Tyr-Trp competitive to succinyl-Leu-Tyr 4-methylcoumarin 7-amide degradation 95372