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

BRENDA support

Literature summary extracted from

  • Xiao, M.; Wang, Y.; Chen, J.; Li, B.
    Characterization of RNA-dependent RNA polymerase activity of CSFV NS5B proteins expressed in Escherichia coli (2003), Virus Genes, 27, 67-74.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.48 full-length enzyme and truncated enzyme forms resulting from deletions of 24, 36, 65 or 82 amino acid residues at the C terminal, with C-terminal hexahistidine tag, expression in Escherichia coli Classical swine fever virus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.48 additional information truncated enzyme forms resulting from deletions of 24, 36, or amino acid residues at the C terminal have RNA-dependent RNA polymerase activity. Truncated enzyme with a deletion of 82 amino acid residues at the C terminal shows no RNA-dependent RNA polymerase activity. Template specificity of the enzyme is not strict wirth NS5B proteins truncated, suggesting that the C terminal of CSFV NS5B protein is involved in the template specificity of the enzyme Classical swine fever virus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Classical swine fever virus
-
 expression in Escherichia coli
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.48 full-length enzyme and truncated enzyme forms resulting from deletions of 24, 36, 65 or 82 amino acid residues at the C terminal, with C-terminal hexahistidine tag Classical swine fever virus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn
-
 Classical swine fever virus diphosphate + RNAn+1
-
 ?