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Literature summary for 2.7.7.48 extracted from

  • Qin, W.; Yamashita, T.; Shirota, Y.; Lin, Y.; Wei, W.; Murakami, S.
    Mutational analysis of the structure and functions of Hepatitis C virus RNA-dependent RNA polymerase (2001), Hepatology, 33, 728-737.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
C274A mutation completely abolishes RNA-dependent RNA polymerase activity Hepacivirus C
E18A mutation completely abolishes RNA-dependent RNA polymerase activity Hepacivirus C
H502A mutation completely abolishes RNA-dependent RNA polymerase activity Hepacivirus C
additional information mutant cm20t in which 7 amino acids in a row are changed to AAASAAA from aa17-23, is totally defective in RNA-dependent RNA polymerase activity Hepacivirus C
additional information mutant cm1940t in which 7 amino acids in a row are changed to AAASAAA from aa191-197, is totally defective in RNA-dependent RNA polymerase activity Hepacivirus C
additional information mutant enzymes cm2t and cm3t are totally defective in RNA-dependent RNA polymerase activity Hepacivirus C
additional information mutant enzyme cm223t in which 7 amino acids in a row are changed to AAASAAA from aa220-226, shows 50% of the activity of the wild-type enzyme Hepacivirus C
Y191A mutation completely abolishes RNA-dependent RNA polymerase activity Hepacivirus C
Y276A mutation completely abolishes RNA-dependent RNA polymerase activity Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
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Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme, wild-type and mutant enzymes, expressed in Escherichia coli Hepacivirus C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn
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 Hepacivirus C diphosphate + RNAn+1
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