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Literature summary extracted from

  • Wang, M.; Ng, K.K.S.; Cherney, M.M.; Chan, L.; Yannopoulos, C.G.; Bedard, J.; Morin, N.; Nguyen-Ba, N.; Alaoui-Ismaili, M.H.; Bethell, R.C.; James, M.N.G.
    Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase (2003), J. Biol. Chem., 278, 9489-9495.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.48 Mg2+ the enzyme requires either Mn2+ or Mg2+ for RNA-dependent RNA polymerase activity. NS5B undergoes conformational changes upon the binding of metal ions. This process does not significantly stimulate the binding to the RNA or NTP substrates Hepacivirus C
2.7.7.48 Mn2+ the enzyme requires either Mn2+ or Mg2+ for RNA-dependent RNA polymerase activity. NS5B undergoes conformational changes upon the binding of metal ions. This process does not significantly stimulate the binding to the RNA or NTP substrates Hepacivirus C

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Hepacivirus C P26663
-
-

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
-
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