EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.113 | D1686G |
mutation does not induce obvious changes in processing |
654012 |
| 3.4.21.113 | D1695A |
mutation does not induce obvious changes in processing |
654012 |
| 3.4.21.113 | H51A |
mutant shows inactivated proteolytic activity |
698763 |
| 3.4.21.113 | K232A |
site-directed mutagenesis, helicase active site mutant |
755207 |
| 3.4.21.113 | K48A |
to prevent its self-cleavage an autolytic site-deficient mutant is generated |
698763 |
| 3.4.21.113 | more |
construction of recombinant full-length NS3 (residues 1 to 683) followed by the 8 N-terminal residues of NS4A, the NS3 sequence is preceeded by residues 21 to 57 of the protease cofactor NS4A |
755207 |
| 3.4.21.113 | more |
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 |
698763 |
| 3.4.21.113 | more |
protease deletion constructs of the helicase domain NS3hel(deltaN166) and NS3hel(deltaN188), which are missing 166 and 188 amino acids, respectively, from the N-terminus of the NS3 protein. NS3hel(deltaN188) binds TS34 RNA, RNA binding by NS3hel(deltaN166) is not detectable |
687647 |
| 3.4.21.113 | more |
the NS3 protease is sensitive to N-terminal truncation because a deletion of 6 amino acids significantly reduces the cleavage efficiency at the NS4A/4B site |
654012 |
| 3.4.21.113 | more |
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 |
698763 |
