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Literature summary extracted from

  • Plotch, S.J.; Palant, O.; Gluzman, Y.
    Purification and properties of Poliovirus RNA polymerase expressed in Escherichia coli (1989), J. Virol., 63, 216-225.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.48 expression in Escherichia coli, a mutant is generated as a result of the deletion of a trinucleotide in the N-terminal portion of the coding region, pT7-POL(TRP-). The protein expressed from this mutant lacks a tryptophan residue normally present at the fifth amino acid from the N-terminal glycine. This protein has no detectable enzymatic activity. Mutant pT7-POL(AvII), which lacks the C-terminal 53 amino acids of the normal protein is also inactive Enterovirus C

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.48 additional information a mutant is generated as a result of the deletion of a trinucleotide in the N-terminal portion of the coding region, pT7-POL(TRP-). The protein expressed from this mutant lacks a tryptophan residue normally present at the fifth amino acid from the N-terminal glycine. This protein has no detectable enzymatic activity. Mutant pT7-POL(AvII), which lacks the C-terminal 53 amino acids of the normal protein is also inactive Enterovirus C

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Enterovirus C
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 expressed in Escherichia coli
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.48
-
 Enterovirus C

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn poly(A)-dependent oligo(U)-primed poly(U) polymerase activity. In the presence of an oligo(U) primer, the enzyme catalyzes the synthesis of a full-length copy of either poliovirus or globin RNA templates. In the absence of added primer, RNA products up to twice the length of the template are synthesized Enterovirus C diphosphate + RNAn+1
-
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