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Literature summary for 2.7.7.48 extracted from

  • Spagnolo, J.F.; Rossignol, E.; Bullitt, E.; Kirkegaard, K.
    Enzymatic and nonenzymatic functions of viral RNA-dependent RNA polymerases within oligomeric arrays (2010), RNA, 16, 382-393.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.48

Application

Application Comment Organism
drug development the functional nature of multimeric arrays of RNA-dependent RNA polymerase supplies a target for antiviral compounds Enterovirus C
pharmacology targeting the active sites of polymerase molecules is not likely to be the best antiviral strategy, as inactivated polymerases do not inhibit replication of other viruses in the same cell and can, in fact, be useful in RNA replication complexes, because catalytically inactive polymerases participate productively in functional oligomer formation and catalysis Enterovirus C
synthesis the functional nature of multimeric arrays of RNA-dependent RNA polymerase provides an appreciation for enzymatic catalysis on membranous surfaces within cells Enterovirus C

Protein Variants

Protein Variants Comment Organism
D328A/D329A site-directed mutagenesis Enterovirus C
D339A/S341A/D349A site-directed mutagenesis, the mutant shows a partial loss of oligomerization with the less severe viral phenotype Enterovirus C
L446N/R455A/R456A site-directed mutagenesis, catalytically complete inactive mutant Enterovirus C
L446N/R455A/R456A/D328A/D329A site-directed mutagenesis, catalytically complete inactive mutant Enterovirus C
additional information generation of mutant 3D polymerase plasmids through splicing by overlapping extension PCR. Mutation of the active site of 3D polymerase does not impede its ability to oligomerize or to participate in functional complexes, the catalytically inactive polymerases participate productively in functional oligomer formation and catalysis. But polymerases containing mutations in the amino terminus, which lead to altered contacts in the folded polymerase and mutations in a known polymerase-polymerase interaction in the two-dimensional protein lattice, cannot participate in functional RNA replication complexes Enterovirus C
R455A/R456A site-directed mutagenesis, catalytically complete inactive mutant Enterovirus C
V33A/F34A site-directed mutagenesis Enterovirus C
V391L naturally occuring mutant, temperature-sensitive mutant. Some function of V391L polymerase other than its catalytic activity can be supplemented at the nonpermissive temperature, most likely via the formation of oligomeric structures on the surface of membranous vesicles that facilitate the tethering of the active enzyme Enterovirus C

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 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
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 activities of wild-type and deletion and point mutation mutant enzymes on HP1 RNA substrate, overview Enterovirus C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn
-
 Enterovirus C diphosphate + RNAn+1
-
 ?
nucleoside triphosphate + RNAn substrate is HP1 RNA Enterovirus C diphosphate + RNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
3D polymerase
-
 Enterovirus C
RNA-dependent RNA polymerases
-
 Enterovirus C

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Enterovirus C

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Enterovirus C

General Information

General Information Comment Organism
physiological function the enzyme is required for replication of the genomes of positive-strand RNA viruses occuring in highly oligomeric complexes on the cytosolic surfaces of the intracellular membranes of infected host cells Enterovirus C