Cloned (Comment) | Organism |
---|---|
recombinant expression in Escherichia coli | Foot-and-mouth disease virus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5-fluorouridine triphosphate | 5-fluorouridine triphosphate is a strong competitive inhibitor of VPg uridylylation by FMDV 3D in vitro, versus UTP, FUTP, dTTP, ATP, CTP, or GTP, uridylylation at VPg Tyr3, which is located near the active site of 3D, at the RNA binding cleft of 3D, binding structure from crystal structure, overview. No inhibition with oligoT primers | Foot-and-mouth disease virus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Foot-and-mouth disease virus | the initiation of FMDV RNA synthesis is strongly inhibited by 5-fluorouridine triphosphate, and it is also an inhibitor of FMDV RNA elongation, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Foot-and-mouth disease virus | - |
i.e. FMDV | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5-fluorouridine triphosphate + RNAn | the enzyme incorporates 5-fluorouridine monophosphate during RNA elongation in place of UMP or CMP using homopolymeric and heteropolymeric templates. Incorporation of 5-fluorouridine monophosphate does not prevent chain elongation, and, in some sequence contexts, it favors misincorporations at downstream positions. 5-Fluorouridine monophosphate is incorporated into the nascent RNA and occupies the new 3'-end of the primer at the active site of the enzyme. 5-Fluorouridine monophosphate establishes a Watson and Crick pair with the corresponding acceptor AMP in the template strand and an additional hydrogen bond with Ser304 of the polymerase. Further interactions, similar to those observed with standard nucleotides, contribute also to stabilize 5-fluorouridine monophosphate in the 3'-terminus of the RNA. When present in the template, 5-fluorouridine monophosphate directs the incorporation of AMP and GMP, with ATP being a more effective substrate than GTP. The misincorporation of GMP is 17fold faster opposite 5-fluorouridine than opposite U in the template. But Incorporated 5-fluorouridine monophosphate is not a chain terminator during RNA elongation | Foot-and-mouth disease virus | diphosphate + RNAn+1 | RNA with incoporated 5-fluorouridine phosphate | ? | |
additional information | the initiation of FMDV RNA synthesis is strongly inhibited by 5-fluorouridine triphosphate, and it is also an inhibitor of FMDV RNA elongation, overview | Foot-and-mouth disease virus | ? | - |
? | |
nucleoside triphosphate + RNAn | purified recombinant FMDV 3D is active in polymerization assays using homopolymeric and heteropolymeric primer templates and in binding to RNA | Foot-and-mouth disease virus | diphosphate + RNAn+1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FMDV 3D | - |
Foot-and-mouth disease virus |
RDRP | - |
Foot-and-mouth disease virus |
RNA-dependent RNA polymerase | - |
Foot-and-mouth disease virus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of inhibition of VPg uridylylation, overview | Foot-and-mouth disease virus |