Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.92 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

Inhibitors Comment Organism Structure
(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
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
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
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
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
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
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
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
304000
-
gel filtration, native enzyme Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
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