Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
foot-and-mouth disease virus capsid precursor (P1-2A) + H2O | Foot-and-mouth disease virus | cleavages at the three junctions (VP0/VP3, VP3/VP1, and VP1/2A) within the foot-and-mouth disease virus capsid precursor (P1-2A) by the 3C protease are mutually independent | foot-and-mouth disease virus protein VP0 + foot-and-mouth disease virus protein VP3 + foot-and-mouth disease virus protein VP1 + foot-and-mouth disease virus protein 2A | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Foot-and-mouth disease virus | - |
FMDV | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
foot-and-mouth disease virus capsid precursor (P1-2A) + H2O | cleavages at the three junctions (VP0/VP3, VP3/VP1, and VP1/2A) within the foot-and-mouth disease virus capsid precursor (P1-2A) by the 3C protease are mutually independent | Foot-and-mouth disease virus | foot-and-mouth disease virus protein VP0 + foot-and-mouth disease virus protein VP3 + foot-and-mouth disease virus protein VP1 + foot-and-mouth disease virus protein 2A | - |
? | |
additional information | the VP2 K217R and VP3 I2P substitutions (near the VP0/VP3 junction of the substrate) strongly reduce the processing at this junction by 3Cpro while the substitution VP2 K217E blocks cleavage. At the VP3/VP1 junction, the substitutions VP3 Q2221P and VP1 T1P each severely inhibit processing at this site. Blocking cleavage at either junction does not prevent processing elsewhere in P1-2A. Processing of the P1-2A precursor in the transient expression assay using BHK cells | Foot-and-mouth disease virus | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
3C protease | - |
Foot-and-mouth disease virus |
General Information | Comment | Organism |
---|---|---|
malfunction | the VP2 K217R and VP3 I2P substitutions (near the VP0/VP3 junction) strongly reduce the processing at this junction by 3Cpro while the substitution VP2 K217E blocks cleavage. At the VP3/VP1 junction, the substitutions VP3 Q2221P and VP1 T1P each severely inhibit processing at this site. Blocking cleavage at either junction does not prevent processing elsewhere in P1-2A. These modifications are also introduced into full-length FMDV RNA revealing that only wild-type and the VP2 K217R mutant are viable | Foot-and-mouth disease virus |