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3.4.21.92: Endopeptidase Clp

This is an abbreviated version!
For detailed information about Endopeptidase Clp, go to the full flat file.

Word Map on EC 3.4.21.92

Reaction

Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs) =

Synonyms

ATP-dependent caseinolytic protease, ATP-dependent Clp protease, ATP-dependent Clp protease proteolytic subunit 1, ATP-dependent Clp protease proteolytic subunit 2, BsClpP, Caseinolytic protease, CLP, Clp protease, Clp proteolytic subunit, ClpA, ClpAP, ClpAP protease, ClpB, ClpC, ClpC ATPase, ClpC1, ClpCP protease, ClpCP3/R protease, ClpE, ClpP, ClpP Peptidase, ClpP Protease, ClpP protease complex, ClpP1, ClpP1 protease, ClpP1P2, ClpP2, ClpP2 protease, ClpP3, ClpP3/R complex, ClpQ, ClpR, ClpS1, ClpX, ClpX2, ClpXP, ClpXP protease, ClpY, CplC, endopeptidase Clp, endopeptidase Ti, Heat shock protein F21.5, heat-shock protease ClpP, nClpP7, nClpP8, PfClpP, Protease Ti, stress protein G7

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.92 Endopeptidase Clp

Inhibitors

Inhibitors on EC 3.4.21.92 - Endopeptidase Clp

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
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
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
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
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
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
3-(4-methoxyphenyl)-4-(pent-4-ynyl)oxetan-2-one
-
shows stronger inhibitory effect
3-(non-8-ynyl)-4-(pent-4-ynyl)oxetan-2-one
-
exerts the weakest effect on peptidase activity
3-butyl-4-(pent-4-ynyl)oxetan-2-one
-
shows stronger inhibitory effect
CAANDENYALAA
-
-
CAANDENYALAA-NH2
-
-
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
-
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
diisopropyl fluorophosphate
diisopropylfluorophosphate
-
fluorosulfonylbenzoyladenosine
-
-
High salt concentrations
-
chloride is much more inhibitory than acetate, divalent anions are also very inhibitory
-
kappa-casein
-
strong, competitive
-
Mg2+
-
proteolytic activity of ClpAP is dependent on, but concentrations higher than about 30 mM are inhibitory
Neohydrin
-
-
phosphoarginine
-
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
Succinyl-Leu-Tyr 4-methylcoumarin 7-amide
-
at high concentrations complete inhibition of casein breakdown
Xaa-Tyr-Leu-Tyr-Trp
-
competitive to succinyl-Leu-Tyr 4-methylcoumarin 7-amide degradation
additional information
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