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Literature summary for 3.4.22.46 extracted from

  • Steinberger, J.; Grishkovskaya, I.; Cencic, R.; Juliano, L.; Juliano, M.A.; Skern, T.
    Foot-and-mouth disease virus leader proteinase: structural insights into the mechanism of intermolecular cleavage (2014), Virology, 468-470, 397-408.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.46

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)LysE cells Foot-and-mouth disease virus

Crystallization (Commentary)

Crystallization (Comment) Organism
isoform sLbpro in complex with inhibitor E-64-R-P-NH2, hanging drop vapor diffusion method, using 0.1 M sodium acetate pH 4.8, 0.9 M NaH2PO4 and 1.2 M K2HPO4 Foot-and-mouth disease virus

Inhibitors

Inhibitors Comment Organism Structure
CA074
-
 Foot-and-mouth disease virus
E64-R-P-NH2
-
 Foot-and-mouth disease virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
eukaryotic initiation factor eIF4G + H2O Foot-and-mouth disease virus in intermolecular cleavage on polyprotein substrates, isoform Lbpro is unaffected by P1 or P1' substitutions and processes a substrate containing nine eIF4GI cleavage site residues whereas isoform sLbpro fails to cleave the eIF4GI containing substrate and cleaves appreciably more slowly on mutated substrates ?
-
 ?

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
eukaryotic initiation factor eIF4G + H2O in intermolecular cleavage on polyprotein substrates, isoform Lbpro is unaffected by P1 or P1' substitutions and processes a substrate containing nine eIF4GI cleavage site residues whereas isoform sLbpro fails to cleave the eIF4GI containing substrate and cleaves appreciably more slowly on mutated substrates Foot-and-mouth disease virus ?
-
 ?
SFANLGRTTL + H2O poor substrate for both isoforms Lbpro and sLbpro Foot-and-mouth disease virus SFANLG + RTTL
-
 ?
VQRKLGAAGQ + H2O isoform sLbpro cleaves this substrate better than isoform Lbpro Foot-and-mouth disease virus VQRKLG + AAGQ
-
 ?
VQRKLGRAGQ + H2O isoform sLbpro cleaves this substrate better than isoform Lbpro Foot-and-mouth disease virus VQRKLG + RAGQ
-
 ?
VQRKLKGAGQ + H2O isoform sLbpro cleaves this substrate better than isoform Lbpro Foot-and-mouth disease virus VQRKLK + GAGQ
-
 ?
VQRKLKRAGQ + H2O isoform sLbpro cleaves this substrate better than isoform Lbpro Foot-and-mouth disease virus VQRKLK + RAGQ
-
 ?

Synonyms

Synonyms Comment Organism
Lbpro isoform Foot-and-mouth disease virus
Leader proteinase
-
 Foot-and-mouth disease virus
Lpro
-
 Foot-and-mouth disease virus
sLbpro during infection, isoform Lbpro removes six residues from its own C-terminus, generating sLbpro Foot-and-mouth disease virus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00003
-
 E64-R-P-NH2 isoform Lbpro, pH and temperature not specified in the publication Foot-and-mouth disease virus
0.0116
-
 CA074 isoform Lbpro, pH and temperature not specified in the publication Foot-and-mouth disease virus