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Literature summary extracted from

  • Grun, J.B.; Brinton, M.A.
    Characterization of West Nile virus RNA-dependent RNA polymerase and cellular terminal adenylyl and uridylyl transferases in cell-free extracts (1986), J. Virol., 60, 1113-1124.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.48 Mn2+ concentrations of 1.0 mM, 0.5 mM and 0.05 mM in the presence of Mg2+ inhibit activity by 75%, 50% and 25%, respectively West Nile virus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.48 Mg2+ Mg2+ is the preferred divalent cation, optimal activity at 3-30 mM West Nile virus
2.7.7.48 Mn2+ 0.05 mM, 40% of the activity compared to reaction with 3 mM Mg2+. 5.0 mM, 70% of the activity compared to the reaction with 3 mM Mg2+, Mn2+ is present as the sole divalent cation West Nile virus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 West Nile virus
-
 BHK cells infected with
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn
-
 West Nile virus diphosphate + RNAn+1
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.48 30 37
-
 West Nile virus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.48 8
-
 in Hepes-NaOH buffer or Tris hydrochloride buffer West Nile virus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.48 7.6 8.4 pH 7.6: about 80% of maximal activity, pH 8.4: about 65% of maximal activity, in Tris hydrochloride buffer West Nile virus