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Literature summary extracted from

  • Kundu, A.; Roychowdhury, A.; Bose, M.; Das, A.K.; Ghosh, A.K.
    Reconstitution of the RNA-dependent RNA polymerase activity of Antheraea mylitta cypovirus in vitro using separately expressed different functional domains of the enzyme (2016), J. Gen. Virol., 97, 1709-1719.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.48 enzyme RNA and amino acid sequence deermination and analysis, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3), recombinant expression of soluble His6-tagged wild-type in High Five cells via the baculovirus expression system Antheraea mylitta cypovirus 4

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.48 D682A site-directed mutagenesis of the central polymerase domain 1 active site residue Antheraea mylitta cypovirus 4
2.7.7.48 D683A site-directed mutagenesis of the central polymerase domain 1 active site residue Antheraea mylitta cypovirus 4

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn Antheraea mylitta cypovirus 4
-
diphosphate + RNAn+1
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Antheraea mylitta cypovirus 4
-
a polyhedrosis virus
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.48 recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) or recombinant soluble His6-tagged wild-type enzyme from High Five insect cells by nickel affinity chromatgraphy to homogeneity Antheraea mylitta cypovirus 4

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 additional information the central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity Antheraea mylitta cypovirus 4 ?
-
?
2.7.7.48 nucleoside triphosphate + RNAn
-
Antheraea mylitta cypovirus 4 diphosphate + RNAn+1
-
?

Subunits

EC Number Subunits Comment Organism
2.7.7.48 More the enzyme has a basic right-handed structure having a palm (residues 520-563, 641-735), thumb (residues 736-879) and fingers (residues 350-519, 564-640) subdomains. The central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity Antheraea mylitta cypovirus 4

Synonyms

EC Number Synonyms Comment Organism
2.7.7.48 RDRP
-
Antheraea mylitta cypovirus 4

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.48 25
-
assay at Antheraea mylitta cypovirus 4

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.48 7.5 8 assay at Antheraea mylitta cypovirus 4

General Information

EC Number General Information Comment Organism
2.7.7.48 physiological function segment 2 (S2)-encoded RNA-dependent RNA polymerase (RdRp) helps the virus to propagate its genome in the host cell of the silkworm, Antheraea mylitta Antheraea mylitta cypovirus 4