EC Number   |
Activating Compound |
Reference |
|---|
   3.2.1.17 | 1,3-dimethylimidazolium iodine |
50% activation at 5% |
728996 |
| 3.2.1.17 | 1-butyl-3-methylimidazolium bromide |
below 20% activation at 5% |
728996 |
| 3.2.1.17 | 1-butyl-3-methylimidazolium chloride |
below 10% activation at 5% |
728996 |
| 3.2.1.17 | 1-butyl-3-methylimidazolium tetrafluoroborate |
below 20% activation at 5% |
728996 |
| 3.2.1.17 | 4-hexylresorcinol |
activates at low concentrations, up to 10-15 molcules of hexylresorcinol per protein globule, but inhibits at higher concentrations, at above 100 molecules of hexylresorcinol per protein globule the activity is abolished |
717301 |
| 3.2.1.17 | 5-methylresorcinol |
interacts with the surface of lysozyme directly, not via water hydrogen bonds. This leads to a decrease in the denaturation temperature and an increase in the amplitude of equilibrium fluctuations, allowing it to be a powerful activator |
717301 |
| 3.2.1.17 | choline |
the cell wall binding module is intrinsically unstable, and the ultimate folding and stabilization of the active, monomeric form of the enzyme relies on choline binding. Complex formation proceeds in a rather slow way, and all sites behave as equivalent. Coupling between choline binding and folding indicates a high conformational plasticity that could correlate with the unusual alternation of short and long choline-binding repeats present in this enzyme. It can contribute to regulate enzymic activity |
698818 |
| 3.2.1.17 | more |
ionic liquids influence protein crystal morphology, size, polymorph, crystal quality, and modify solution properties, possible mechanisms, overview |
728996 |
| 3.2.1.17 | more |
no activation by 2-mercaptoethanol |
696020 |
| 3.2.1.17 | more |
practically inactive in absence of Triton X-100, hydrolysis of murein catalysed only when in contact with lipophilic components |
171048 |
