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Literature summary for 2.7.7.48 extracted from

  • Kim, H.; Ellis, V.D.; Woodman, A.; Zhao, Y.; Arnold, J.J.; Cameron, C.E.
    RNA-dependent RNA polymerase speed and fidelity are not the only determinants of the mechanism or efficiency of recombination (2019), Genes (Basel), 10, 968 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
IF-KH I331F/K359H the mutant is competent for copy-choice recombination Enterovirus C
IF-PS-KH I331F/P356S/K359H the triple mutant replicates even faster but still exhibits a significant reduction in the rate of replication relative to wild-type enzyme. The virus is impaired substantially for recombination in cells Enterovirus C
K359H the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type. K359H poliovirus is genetically unstable and acquires mutations encoding two second-site amino acid substitutions after a few passages in cell cultures Enterovirus C
K359R the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type Enterovirus C
PS-KH P356S/K359H the mutant is competent for forced-copy-choice recombination Enterovirus C

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nucleoside triphosphate + RNAn Enterovirus C
-
 diphosphate + RNAn+1
-
 ?

Organism

Organism UniProt Comment Textmining
Enterovirus C
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn
-
 Enterovirus C diphosphate + RNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
RDRP
-
 Enterovirus C
RNA-dependent RNA polymerase
-
 Enterovirus C