EC Number   |
Activating Compound |
Reference |
|---|
   3.4.21.98 | 4A cofactor peptide |
- |
717962 |
| 3.4.21.98 | DTT |
required for maximal activity |
81445 |
| 3.4.21.98 | glycerol |
- |
681172 |
| 3.4.21.98 | more |
both auto-cleavage and NS3 protease activity show absolute requirement for cysteine residues 1123, 1125 and 1171 within NS3. Cysteine 922 (within NS2) is only required for NS2/3 auto-cleavage activity and histidine 1175 is only required for NS3 activity. Complete NS3 protease domain (including the C-terminal alpha-helix) is required for NS2/3 auto-cleavage, the activity of the NS3 protease is not essential |
681415 |
| 3.4.21.98 | NS4A |
- |
650830 |
| 3.4.21.98 | NS4A |
cofactor for efficient for efficient cleavage at four sites in the nonstructural region, biological importance of the NS4A N-terminus, in fully potentiating NS3 enzymatic activity |
649548 |
| 3.4.21.98 | NS4A |
enhances the activity of NS3 protease in all cleavages via the formation of an NS3/NS4A |
81432, 81435, 81437, 81439, 81446 |
| 3.4.21.98 | NS4A |
hydrophobic central core of NS4A corresponding to residues 21-34, kinetic value for a modified peptide modified with a KK residue at the C-terminus to enhance solubility, Km: 0.00076 mM, kcat: 9 per min |
81435 |
| 3.4.21.98 | NS4A |
NS4A is a 54 residue amphipathic peptide acting as a cofactor and possibly assisting the membrane-localization of NS3 |
81432 |
| 3.4.21.98 | NS4A cofactor peptide |
NS3-NS4A interaction consists of a high-affinity and a low-affinity interaction, contributing equally to the overall binding. By immobilizing NS3 alone or together with NS4A it is shown that inhibitors have a higher affinity for NS3 in the presence of NS4A. NS4A thus has a direct effect on the binding of inhibitors to NS3 and not only on catalysis |
718016 |
