Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy

Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys!Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly!Arg- and -Lys!Arg-

Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses. Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue. The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory. Type example of peptidase family C28.

EC 3.4.22.46 created 2001

1  [PMID:7609064]

Piccone ME, Zellner M, Kumosinski TF, Mason PW, Grubman MJ.

Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus.

J Virol 69:4950-6 (1995)
DOI:10.1128/JVI.69.8.4950-4956.1995

2  [PMID:11183785]

Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T

Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes.

J Mol Biol 302:1227-40 (2000)
DOI:10.1006/jmbi.2000.4115

[ag:CAA25416]