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Literature summary for 2.7.7.48 extracted from

  • Arnold, J.J.; Gohara, D.W.; Cameron, C.E.
    Poliovirus RNA-dependent RNA polymerase (3Dpol): pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mn2+ (2004), Biochemistry, 43, 5138-5148.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ using Mg2+ as the divalent cation cofactor, the enzyme can use both the first conformational-change step and the phosphoryl-transfer step to distinguish between correct and incorrect nucleotides Enterovirus C
Mn2+ using Mn2+ as the cofactor, the ability to diminish the rate of phosphoryl transfer for incorrect nucleotides relative to correct nucleotides is lost completely, leaving only the conformational-change step for selection of the correct nucleotide Enterovirus C

Organism

Organism UniProt Comment Textmining
Enterovirus C
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-
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Synonyms

Synonyms Comment Organism
RNA-dependent RNA polymerase
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Enterovirus C