KEGG   ENZYME: 3.4.22.46Help
Entry
EC 3.4.22.46                Enzyme                                 

Name
L-peptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
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-
Comment
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.
History
EC 3.4.22.46 created 2001
Reference
1  [PMID:7609064]
  Authors
Piccone ME, Zellner M, Kumosinski TF, Mason PW, Grubman MJ.
  Title
Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus.
  Journal
J. Virol. 69 (1995) 4950-6.
  Organism
foot-and-mouth disease virus
Reference
2  [PMID:11183785]
  Authors
Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T.
  Title
Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes.
  Journal
J. Mol. Biol. 302 (2000) 1227-40.
  Organism
foot-and-mouth disease virus
  Sequence
[up:P03305]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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