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Literature summary for 2.7.7.48 extracted from

  • Lohmann, V.; Korner, F.; Herian, U.; Bartenschlager, R.
    Biochemical properties of Hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymic activity (1997), J. Virol., 71, 8416-8428.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
NS5B-hexahistidine fusion protein expressed with recombinant baculoviruses in insect Sf9 cells Hepacivirus C

Protein Variants

Protein Variants Comment Organism
additional information deletion of only 19 amino acids from the amino terminus severely reduces the polymerase activity, which is completely abolished when 40 amino acids are removed. Truncations from the carboxy terminus are less deleterious Hepacivirus C

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Hepacivirus C
Mn2+
-
 Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
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-
-

Purification (Commentary)

Purification (Comment) Organism
NS5B-hexahistidine fusion protein expressed with recombinant baculoviruses in insect Sf9 cells Hepacivirus C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn RNA-dependent RNA polymerase activity uses poly(C) most efficiently as a template but is inactive on poly(U) and poly(G). The enzyme is able to copy a full-length or nearly full-length genome in the absence of additional viral or cellular cofactors. Poly(C)-oligo(G)12 is the most efficient substrate Hepacivirus C diphosphate + RNAn+1
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