EC Number   |
Inhibitors |
Structure |
|---|
   3.5.1.52 | 2-mercaptoethanol |
20% inhibition at 100 mM |
   |
| 3.5.1.52 | benzyloxycarbonyl-VAD-fluoromethyl ketone |
- |
|
| 3.5.1.52 | benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone |
covalently bind to the active site Cys191 of recombinant yeast peptide N-glycanase |
|
| 3.5.1.52 | Ca2+ |
2 mM, 19% inhibition |
|
| 3.5.1.52 | carbobenzyloxy-Val-Ala-Asp |
i.e. Z-VAD, binds to the active site of the enzyme, binding structure, overview |
|
| 3.5.1.52 | carbobenzyloxy-Val-Ala-Asp |
i.e. Z-VAD, in vivo inhibition |
|
| 3.5.1.52 | carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone |
i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, binds covalently to the active site of the mammalian enzyme, in vivo inhibition of recombinant PNGase in U373 cells, overview |
|
| 3.5.1.52 | carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone |
i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, binds covalently to the active site of the mammalian enzyme |
|
| 3.5.1.52 | carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone |
i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, IC50: 0.05 mM, binds covalently to the active site of the yeast enzyme, no restoration of enzyme activity by dialysis |
|
| 3.5.1.52 | carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone |
i.e. Z-VAD-fmk, in vivo inhibition |
|
