EC Number   |
Activating Compound |
Reference |
|---|
   3.4.25.2 | 1-(3,4-dihydroxyphenyl)-2-[2-(pyridin-2-yl)-1H-benzimidazol-1-yl]ethanone |
- |
733478 |
| 3.4.25.2 | 1-(4-nitrophenyl)-2-[2-(pyridin-2-yl)-1H-benzimidazol-1-yl]ethanone |
- |
733478 |
| 3.4.25.2 | 3-{(E)-[(2-hydroxynaphthalen-1-yl)methylidene]amino}-2-(4-nitrophenyl)quinazolin-4(3H)-one |
- |
733478 |
| 3.4.25.2 | HslU |
HslV can be activated by binding of a hexameric HslU(DELTAI)6 ring lacking the I domain. The activation is effected through a conformational change in hslV rather than through alteration of the size of the entry channel into the protease catalytic cavity. The two HslV6 rings in the protease dodecamer are activated independently rather than cooperatively |
647891 |
| 3.4.25.2 | HslU |
HslV can slowly hydrolyze insulin B-chain, casein or carboxymethylated lactalbumin, but its activity is stimulated 20fold by HslU in presence of ATP |
647889 |
| 3.4.25.2 | HslU |
HslV protomer interfaces perform distinct functions: whereas intra-ring interface participates in HslV:HslU interaction resulting in allosteric activation of HslV protease by HslU, the interring interfaces uphold the oligomeric form of HslV |
689884 |
| 3.4.25.2 | HslU |
protease HslV is activated by the ATPase HslU. Mutations in hslV that disrupt the interaction with the C termini of HslU invariably lead to inactive enzyme |
647890 |
| 3.4.25.2 | HslU |
the HslU C-terminal tails act as a molecular switch for the assembly of HslVU complex and the activation of HslV peptidase |
647878 |
| 3.4.25.2 | HslU ATPase |
natural activator |
733478 |
| 3.4.25.2 | more |
protease HslV can be activated by peptides derived from the C-termini of both ATPase isoforms HslU1 and HslU2. Five out of the six C-terminal residues of HslU2 are essential for binding to and activating HslV. Dodecapeptides derived from HslU of other parasites and bacteria are able to activate HslV with similar or even higher efficiency |
753921 |
