Literature summary for 3.4.22.46 extracted from

Mayer, C.; Neubauer, D.; Nchinda, A.T.; Cencic, R.; Trompf, K.; Skern, T.
Residue L143 of the foot-and-mouth disease virus leader proteinase is a determinant of cleavage specificity (2008), J. Virol., 82, 4656-4659.

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Protein Variants

Protein Variants	Comment	Organism
L143A	self-processes efficiently at the L(pro)/VP4 cleavage site containing P2 phenylalanine, self-processing at the eIF4GII sequence Asp-Phe-Gly-Arg-Gln-Thr is improved but shows more-extensive aberrant processing	Foot-and-mouth disease virus
L143M	does not self-process efficiently at the L(pro)/VP4 cleavage site containing P2 phenylalanine	Foot-and-mouth disease virus
additional information	leader proteinase self-processes inefficiently at the L(pro)/VP4 cleavage site Lys-Leu-Lys-Gly-Ala-Gly when the leucine at position P2 is replaced by phenylalanine: Molecular modeling and energy minimization identifies the L(pro) residue L143 as being responsible for this discrimination	Foot-and-mouth disease virus

Organism

Organism	UniProt	Comment	Textmining
Foot-and-mouth disease virus	P03305	-	-

Synonyms

Synonyms	Comment	Organism
Leader proteinase	-	Foot-and-mouth disease virus
Lpro	-	Foot-and-mouth disease virus

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Release 2023.1 (January 2023)