Cloned (Comment) | Organism |
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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 | Comment | Organism |
---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Enterovirus C | - |
expressed in Escherichia coli | - |
Purification (Comment) | Organism |
---|---|
- |
Enterovirus C |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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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