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Literature summary for 3.4.21.98 extracted from
- In-cell selectivity profiling of membrane-anchored and replicase-associated hepatitis C virus NS3-4A protease reveals a common, stringent substrate recognition profile (2011), Biol. Chem., 392, 927-935.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Huh-7 cells | Hepacivirus C |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hepacivirus C | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | comparison of the cleavage efficiencies of all known HCV NS3-4A cleavage sequences in a cell-based system is reported. NS4B/NS5A and NS5A/NS5B are both processed efficiently in trans, in contrast to NS3/NS4A and NS4A/NS4B, which are not processed significantly above background. ER-anchoring of the substrate is critical for its cleavage by NS3-4A. Other HCV proteins or replicase components do not change NS3-4A substrate selectivity or activity | Hepacivirus C | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NS3-4A protease | - |
Hepacivirus C |
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