General Stability | Organism |
---|---|
the EF-Tu*Ts complex rather than the individual polypeptides functions in the renaturation of Qbeta replicase, treatment of pure EF-Tu with kiromycin prevents it from functioning in the renaturation of Qbeta replicase | Qubevirus durum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
delvomycin | the protein synthetic activity of the EF-Tu in the replicase complex is eliminated but the Qbeta RNA replicase activity is only slightly affected | Qubevirus durum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | Qubevirus durum | composed of one phage-coded polypeptide and three host-supplied polypeptides which function in the biosynthesis of proteins in the uninfected host. Two of theses polypeptides, protein elongation factors EF-Tu and EF-Ts, are required for initiation of transcription by replicase with all templates | diphosphate + RNAn+1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Qubevirus durum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | - |
Qubevirus durum | diphosphate + RNAn+1 | - |
? | |
nucleoside triphosphate + RNAn | composed of one phage-coded polypeptide and three host-supplied polypeptides which function in the biosynthesis of proteins in the uninfected host. Two of theses polypeptides, protein elongation factors EF-Tu and EF-Ts, are required for initiation of transcription by replicase with all templates | Qubevirus durum | diphosphate + RNAn+1 | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | composed of one phage-coded polypeptide and three host-supplied polypeptides | Qubevirus durum |