Entry |
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Name |
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Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
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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-
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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.
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History |
EC 3.4.22.46 created 2001
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Reference |
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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 |
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Reference |
|
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 |
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Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 3.4.22.46 |
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