L-peptidase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.46 L-peptidase
L-peptidase is a cysteine protease best known from foot-and-mouth disease virus but also occurring in other aphthoviruses and cardioviruses. By destroying the host translation initiation factor eIF-4G, it shuts off host-cell protein synthesis while allowing synthesis of viral proteins to continue. Its tertiary structure reveals a distant relationship to papain and, consistently, compound E-64 is inhibitory; it is the type example of peptidase family L. It autocatalytically cleaves itself from the viral polyprotein by hydrolysis of a Lys-/-Gly bond, and then cleaves host eIF-4G at -Gly-/-Arg- and -Lys-/-Arg- bonds. In the virus it remodels host translation machinery. It features a papain-related catalytic fold adapted for eIF4G cleavage.
L-peptidase is a cysteine protease best known from foot-and-mouth disease virus but also occurring in other aphthoviruses and cardioviruses. By destroying the host translation initiation factor eIF-4G, it shuts off host-cell protein synthesis while allowing synthesis of viral proteins to continue. Its tertiary structure reveals a distant relationship to papain and, consistently, compound E-64 is inhibitory; it is the type example of peptidase family L. It autocatalytically cleaves itself from the viral polyprotein by hydrolysis of a Lys-/-Gly bond, and then cleaves host eIF-4G at -Gly-/-Arg- and -Lys-/-Arg- bonds. In the virus it remodels host translation machinery. It features a papain-related catalytic fold adapted for eIF4G cleavage.
References:
Biomedical Dictionary
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