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Literature summary for 3.4.22.28 extracted from

  • Kristensen, T.; Newman, J.; Guan, S.H.; Tuthill, T.J.; Belsham, G.J.
    Cleavages at the three junctions within the foot-and-mouth disease virus capsid precursor (P1-2A) by the 3C protease are mutually independent (2018), Virology, 522, 260-270 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Foot-and-mouth disease virus
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FMDV
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Substrates and Products (Substrate)

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
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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

Synonyms Comment Organism
3C protease
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Foot-and-mouth disease virus

General Information

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