EC Number |
Inhibitors |
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 |
|
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 |
|
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 |
|
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 |
|
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 |
|
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 |
|
3.4.21.92 | 3-(4-methoxyphenyl)-4-(pent-4-ynyl)oxetan-2-one |
shows stronger inhibitory effect |
|
3.4.21.92 | 3-(non-8-ynyl)-4-(pent-4-ynyl)oxetan-2-one |
exerts the weakest effect on peptidase activity |
|
3.4.21.92 | 3-butyl-4-(pent-4-ynyl)oxetan-2-one |
shows stronger inhibitory effect |
|
3.4.21.92 | CAANDENYALAA |
- |
|