Application | Comment | Organism |
---|---|---|
drug development | genotype 1a, different catalytic efficiencies among NS3/4A proteases from different or similar hepatitis C virus genotypes. Because modulation of enzymatic activity of the protease is dependent on the interactions of a small number of NS4A amino acid residues, the design of small peptidomimetic protease inhibitors may be feasible | Hepacivirus C |
drug development | genotype 1b, different catalytic efficiencies among NS3/4A proteases from different or similar hepatitis C virus genotypes. Because modulation of enzymatic activity of the protease is dependent on the interactions of a small number of NS4A amino acid residues, the design of small peptidomimetic protease inhibitors may be feasible | Hepacivirus C |
drug development | genotype 3a, different catalytic efficiencies among NS3/4A proteases from different or similar hepatitis C virus genotypes. Because modulation of enzymatic activity of the protease is dependent on the interactions of a small number of NS4A amino acid residues, the design of small peptidomimetic protease inhibitors may be feasible | Hepacivirus C |
drug development | genotype 4a, different catalytic efficiencies among NS3/4A proteases from different or similar hepatitis C virus genotypes. Because modulation of enzymatic activity of the protease is dependent on the interactions of a small number of NS4A amino acid residues, the design of small peptidomimetic protease inhibitors may be feasible | Hepacivirus C |
drug development | genotype 4d, different catalytic efficiencies among NS3/4A proteases from different or similar hepatitis C virus genotypes. Because modulation of enzymatic activity of the protease is dependent on the interactions of a small number of NS4A amino acid residues, the design of small peptidomimetic protease inhibitors may be feasible | Hepacivirus C |
Cloned (Comment) | Organism |
---|---|
Escherichia coli JM109 cells containig plasmid pcI.HCVcro that includes the NS5A/NS5B cleavage site transformed with plasmid pHCVNS32-181/421-34 protease. Expression in Escherichia coli XL-1 Blue cells | Hepacivirus C |
Escherichia coli JM109 cells containing plasmid pcI.HCVcro that includes the NS5A/NS5B cleavage site transformed with plasmid pHCVNS32-181/421-34 protease. Expression in Escherichia coli XL-1 Blue cells | Hepacivirus C |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hepacivirus C | - |
- |
- |
Hepacivirus C | A8DX91 | - |
- |
Hepacivirus C | A8DXI7 | - |
- |
Hepacivirus C | A8DXT5 | - |
- |
Hepacivirus C | B0L492 | - |
- |
Hepacivirus C | B0L493 | - |
- |
Hepacivirus C | B0L494 | - |
- |
Hepacivirus C | B0L495 | - |
- |
Hepacivirus C | B0L496 | - |
- |
Hepacivirus C | B0L497 | - |
- |
Hepacivirus C | Q8JRC7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 123% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 165% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 23.5% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 38.4% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 39.1% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 53.2% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 58.8% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 68.4% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 70.6% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 72.6% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 73.9% catalytic efficiency | Hepacivirus C | ? | - |
? | |
Hepatitis virus C polyprotein NS5A/NS5B + H2O | 86.5% catalytic efficiency | Hepacivirus C | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NS3/4A protease | - |
Hepacivirus C |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | enhancement of NS3 catalytic efficiency by the NS4A cofactor depends on a few specific amino acid residues | Hepacivirus C |