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 | 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Enterovirus C |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | Enterovirus C | - |
diphosphate + RNAn+1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Enterovirus C | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
3D polymerase | - |
Enterovirus C |
RNA-dependent RNA polymerases | - |
Enterovirus C |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Enterovirus C |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Enterovirus C |
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 |