Literature summary for 2.7.7.48 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.

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

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

Organism	UniProt	Comment	Textmining
Enterovirus C	-	expressed in Escherichia coli	-

Purification (Commentary)

Purification (Comment)	Organism
-	Enterovirus C

Substrates and Products (Substrate)

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	-	?