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Literature summary for 2.7.7.88 extracted from

  • Ogino, T.; Banerjee, A.K.
    The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity (2010), J. Gen. Virol., 91, 1311-1314.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Chandipura virus

Protein Variants

Protein Variants Comment Organism
H1217A mutant is completely inactive in RNA capping Chandipura virus
H1226A no loss of activity Chandipura virus
R1211A mutant is completely inactive in RNA capping Chandipura virus
R1218A mutant is completely inactive in RNA capping Chandipura virus

Organism

Organism UniProt Comment Textmining
Chandipura virus P13179
-
-
Chandipura virus I653514 P13179
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-triphospho-mRNA + GDP
-
Chandipura virus diphosphate + guanosine 5'-triphospho-mRNA
-
?
5'-triphospho-mRNA + GDP
-
Chandipura virus I653514 diphosphate + guanosine 5'-triphospho-mRNA
-
?

Synonyms

Synonyms Comment Organism
RNA-directed RNA polymerase L
-
Chandipura virus

General Information

General Information Comment Organism
physiological function RNA polymerase L protein shows RNA:GDP polyribonucleotidyltransferase activity, which transfers the 5'-monophosphorylated viral mRNA start sequence to GDP to produce a capped RNA. The conserved HR motif in the L protein is essential for the this activity. L protein forms two distinct SDS-resistant complexes with the mRNA and leader RNA start sequences, mutations in the HR motif significantly reduce the formation of the former complex, but not the latter complex Chandipura virus