Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | West Nile virus |
Protein Variants | Comment | Organism |
---|---|---|
H51A | mutant shows inactivated proteolytic activity | West Nile virus |
K48A | to prevent its self-cleavage an autolytic site-deficient mutant is generated | West Nile virus |
additional information | it is shown that both NS3 helicase and NS3 proteinase-helicase constructs are capable of unwinding both the DNA and the RNA templates. In contrast, the full-length NS2B-NS3 proteinase-helicase unwinds only the RNA templates, whereas its DNA unwinding activity is severely repressed | West Nile virus |
additional information | using a construct consisting of the upstram NS2B sequence and the proteinase domain bearing a K48A mutation followed by the helicase domain and another constrcut lacking the helicase domain it is shown that the helicase domain does not significantly affect the proteolytic activity | West Nile virus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
West Nile virus | Q3HM13 | - |
- |
Purification (Comment) | Organism |
---|---|
using HiTrap Co2+-chelating chromatography | West Nile virus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O | - |
West Nile virus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NS3 proteinase | - |
West Nile virus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | West Nile virus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the presence of the upstream virus-encoded NS2B cofactor is required for NS3 proteinase to exhibit its functional activity | West Nile virus |