Application | Comment | Organism |
---|---|---|
drug development | the enzym eis a target for inhibitor design for inhibition of viral replication | Foot-and-mouth disease virus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CA074 | epoxide-based inhibitor of cysteine proteinases, two-step overall irreversible inhibition, with step one being reversible and step two irreversible | Foot-and-mouth disease virus | |
E64 | epoxide-based inhibitor of cysteine proteinases, two-step overall irreversible inhibition, with step one being reversible and step two irreversible. Extending E64 by addition of the dipeptide R-P to a compound termed E64-R-P-NH2, which irreversibly inhibits Lbpro with a Ki of 30 nM and k4 of 0.01/min, can serve as the basis for design of specific inhibitors of FMDV replication | Foot-and-mouth disease virus | |
E64-R-P-NH2 | extending E64 by addition of the dipeptide R-P to a compound termed E64-R-P-NH2, which irreversibly inhibits Lbpro with a Ki of 30 nM and k4 of 0.01/min, can serve as the basis for design of specific inhibitors of FMDV replication | Foot-and-mouth disease virus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
eukaryotic initiation factor 4G + H2O | Foot-and-mouth disease virus | Lbpro cleaves two homologues of the host cell protein. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7 | ? | - |
? | |
additional information | Foot-and-mouth disease virus | the leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Lbpro is not only one of the smallest papain-like cysteine peptidases but also one of the most specific. It has high prime side specificity at least down to the S' 5 site. It can still however cleave between both K-G and G-R pairs | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Foot-and-mouth disease virus | - |
FMDV | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abz-KLKGAGQ-EDDnp + H2O | hydrolysis of FRET peptides | Foot-and-mouth disease virus | Abz-KLK + GAGQ-EDDnp | - |
? | |
eukaryotic initiation factor 4G + H2O | Lbpro cleaves two homologues of the host cell protein. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7 | Foot-and-mouth disease virus | ? | - |
? | |
additional information | the leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Lbpro is not only one of the smallest papain-like cysteine peptidases but also one of the most specific. It has high prime side specificity at least down to the S' 5 site. It can still however cleave between both K-G and G-R pairs | Foot-and-mouth disease virus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Lbpro | - |
Foot-and-mouth disease virus |
leader protease | - |
Foot-and-mouth disease virus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Foot-and-mouth disease virus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Foot-and-mouth disease virus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics mechanism of two-step overall irreversible inhibition by cysteinase inhibitors | Foot-and-mouth disease virus | |
0.00003 | - |
E64-R-P-NH2 | pH 7.8, 37°C | Foot-and-mouth disease virus | |
0.0034 | - |
E64 | pH 7.8, 37°C | Foot-and-mouth disease virus | |
0.0116 | - |
CA074 | pH 7.8, 37°C | Foot-and-mouth disease virus |
General Information | Comment | Organism |
---|---|---|
physiological function | foot and mouth disease virus expresses its genetic information as a single polyprotein that is translated from the single-stranded RNA genome. The leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Subsequently, Lbpro cleaves the two homologues of the host cell protein eukaryotic initiation factor 4G, eIF4G. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7 | Foot-and-mouth disease virus |