ENZYME entry: EC 3.4.22.46

Accepted Name
L-peptidase.
Reaction catalysed
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(s)
  • 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.
  • Belongs to peptidase family C28.
Cross-references
BRENDA3.4.22.46
EC2PDB3.4.22.46
ExplorEnz3.4.22.46
PRIAM enzyme-specific profiles3.4.22.46
KEGG Ligand Database for Enzyme Nomenclature3.4.22.46
IUBMB Enzyme Nomenclature3.4.22.46
IntEnz3.4.22.46
MEDLINEFind literature relating to 3.4.22.46
MetaCyc3.4.22.46
UniProtKB/Swiss-Prot
P03306, POLG_FMDV1;  P03307, POLG_FMDV5;  P03308, POLG_FMDVA;  
P03309, POLG_FMDVC;  P03310, POLG_FMDVI;  P03305, POLG_FMDVO;  
P03311, POLG_FMDVS;  P15072, POLG_FMDVT;  P49303, POLG_FMDVZ;  

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