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Literature summary for 3.4.21.113 extracted from

  • Chernov, A.V.; Shiryaev, S.A.; Aleshin, A.E.; Ratnikov, B.I.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
    The two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase (2008), J. Biol. Chem., 283, 17270-17278.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein West Nile virus

Protein Variants

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

Organism UniProt Comment Textmining
West Nile virus Q3HM13
-
-

Purification (Commentary)

Purification (Comment) Organism
using HiTrap Co2+-chelating chromatography West Nile virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
-
West Nile virus ?
-
?

Synonyms

Synonyms Comment Organism
NS3 proteinase
-
West Nile virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at West Nile virus

Cofactor

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