EC Number   |
Inhibitors |
Structure |
|---|
   3.4.25.2 | 3,4-dichloroisocoumarin |
0.2 mM, 50% inhibition |
   |
| 3.4.25.2 | acety-Leu-Leu-norleucinal |
0.01 mM, 90% inhibition |
|
| 3.4.25.2 | ADP |
when added together with ATP |
|
| 3.4.25.2 | ATP |
inhibits the degradation of unfolded proteins by HslV |
|
| 3.4.25.2 | ATP |
inhibits the degradation of unfolded proteins by HslV. This inhibitory effect of ATP is markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly, suggesting that interaction of ATP with the Arg residue blocks access of unfolded proteins to the proteolytic chamber of HslV |
|
| 3.4.25.2 | benzyloxycarbonyl-Ile-Glu(tert-butyl)-Ala-Leu-al |
0.001 mM, almost complete inhibition of peptidase activity, no inhibition of hydrolysis of insulin B-chain or other polypeptide substrates |
|
| 3.4.25.2 | benzyloxycarbonyl-Leu-Leu-norleucinal |
0.01 mM, 97% inhibition |
|
| 3.4.25.2 | benzyloxycarbonyl-Leu-Leu-norvalinal |
0.004 mM, inhibits hydrolysis of both benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin and insulin B-chain to a similar extent |
|
| 3.4.25.2 | diisopropyl fluorophosphate |
10 mM, about 70% inhibition |
|
| 3.4.25.2 | dithiothreitol |
- |
|
