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 69:4950-6 (1995)
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 302:1227-40 (2000)
DOI:10.1006/jmbi.2000.4115
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.46
IUBMB Enzyme Nomenclature: 3.4.22.46
ExPASy - ENZYME nomenclature database: 3.4.22.46
BRENDA, the Enzyme Database: 3.4.22.46

DBGET integrated database retrieval system