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Literature summary extracted from

  • Vo, N.V.; Tuler, J.R.; Lai, M.M.C.
    Enzymatic characterization of the full-length and C-terminally truncated Hepatitis C virus RNA polymerases: function of the last 21 amino acids of the C terminus in template binding and RNA synthesis (2004), Biochemistry, 43, 10579-10591.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.48 additional information removal of the C21 domain enhances the enzyme stability. Whereas RNA synthesis by the full-length enzyme remains relatively constant at 12-100 mM KCl, synthesis by DELTA21 truncation mutatnt rapidly decreases at KCl concentrations greater than 12 mM. Binding by DELTA21 mutant but not full-length enzyme decreases proportionally as the KCl concentration increases from 25 to 200 mM. The truncation mutant becomes severely inhibited at elevated NTP concentrations, which most likely is due to competitive binding of the noncomplementary nucleotide to the polymerase catalytic center Hepacivirus C

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn Hepacivirus C
-
 diphosphate + RNAn+1
-
 ?

Organism

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.7.7.48 NS5B RdRp
-
 Hepacivirus C