Literature summary for 3.4.21.89 extracted from

Guarne, A.; Hampoelz, B.; Glaser, W.; Carpena, X.; Torma, J.; Fita, I.; Skern, T.
Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes (2000), J. Mol. Biol., 302, 1227-1240.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Foot-and-mouth disease virus

Crystallization (Commentary)

Crystallization (Comment)	Organism
cubic crystalsdifferent variants, Lbpro-C51A, space group P4(1)32, unit cell a : 275.5 A, sLbpro-C51A-C133S, space group P2(1), a : 46.0, b : 110.8, c : 57.0	Foot-and-mouth disease virus

Protein Variants

Protein Variants	Comment	Organism
C51A	Lbpro mutant, site-directed mutagenesis	Foot-and-mouth disease virus
C51A/C133S	Lbpro-double mutant, site-directed mutagenesis	Foot-and-mouth disease virus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
signal peptides from preproteins + H2O	Foot-and-mouth disease virus	-	mature proteins	-	?

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
Lbpro-C51A, Lbpro-C51A-C-133S, and sLbpro-C51A-C133S	Foot-and-mouth disease virus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
signal peptides from preproteins + H2O	-	Foot-and-mouth disease virus	mature proteins	-	?

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Release 2023.1 (January 2023)