Any feedback?
Literature summary for 3.4.21.98 extracted from
- Mechanistic and kinetic characterization of hepatitis C virus NS3 protein interactions with NS4A and protease inhibitors (2011), J. Mol. Recognit., 24, 60-70.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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 | Hepacivirus C |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hepacivirus C | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Ac-Asp-Glu-Asp(EDANS)-Glu-Glu-Abu-PSI[COO]Ala-Ser-Lys(DABCYL) + H2O | - |
Hepacivirus C | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NS3 | - |
Hepacivirus C |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Hepacivirus C |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Hepacivirus C |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
