Literature summary for 2.7.7.48 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.

Search for more literature for 2.7.7.48

Cloned(Commentary)

Cloned (Comment)	Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?
nucleoside triphosphate + RNAn	-	Antheraea mylitta cypovirus 4	diphosphate + RNAn+1	-	?

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
RDRP	-	Antheraea mylitta cypovirus 4

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information	Comment	Organism
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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)