Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.48 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Hepacivirus C
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 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
-
 ?