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Literature summary extracted from

  • Gersch, M.; Kolb, R.; Alte, F.; Groll, M.; Sieber, S.A.
    Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition (2014), J. Am. Chem. Soc., 136, 1360-1366.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
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 Staphylococcus aureus
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 Staphylococcus aureus
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 Staphylococcus aureus
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 Staphylococcus aureus
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 Staphylococcus aureus
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 Staphylococcus aureus
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 Staphylococcus aureus
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 Staphylococcus aureus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.92 150000
-
 gel filtration, enzyme treated with inhibitor diisopropyl fluorophosphate, 1-[4-(4-ethynylbenzoyl)-1,1-dioxido-1,2-thiazetidin-2-yl]undec-10-en-1-one, or beta-lactone (4R)-3-(4-methoxyphenyl)-4-(pent-4-yn-1-yl)oxetan-2-one Staphylococcus aureus
3.4.21.92 304000
-
 gel filtration, native enzyme Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.92 Staphylococcus aureus
-
-
-

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.4.21.92 98
-
 pH not specified in the publication, temperature not specified in the publication Staphylococcus aureus 1-[4-(4-ethynylbenzoyl)-1,1-dioxido-1,2-thiazetidin-2-yl]ethanone