tetX LC cleaves target cell VAMP2

Stable Identifier
Reaction [transition]
Homo sapiens
Related Species
Clostridium tetani
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Tetanus toxin light chain (tetX LC), in the cytosol of a target cell, catalyzes the removal of an aminoterminal peptide from vesicle-associated membrane protein 2 (VAMP2). tetX LC is a zinc metalloprotease (Foran et al. 1994; Schiavo et al. 1992). VAMP2 is associated with the cytosolic face of the target cell synaptic vesicle and is required for vesicle docking and exocytosis. Its cleavage by botulinum toxin blocks exocytosis and in vivo leads to a long-lasting spastic paralysis (Link et al. 1992).
Literature References
PubMed ID Title Journal Year
1361727 Tetanus toxin action: inhibition of neurotransmitter release linked to synaptobrevin proteolysis

S├╝dhof, TC, Baumert, M, Yamasaki, S, Link, E, Niemann, H, Eisel, U, Binz, T, Jahn, R, Edelmann, L, Chou, JH

Biochem. Biophys. Res. Commun. 1992
7803399 Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments

Shone, CC, Foran, P, Dolly, JO

Biochemistry 1994
1396558 Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc

Poulain, B, Schiavo, G, Montecucco, C, Rossetto, O, Benfenati, F, Tauc, L

EMBO J. 1992
Catalyst Activity

metalloendopeptidase activity of tetX LC:Zn2+ [cytosol]

Name Identifier Synonyms
tetanus DOID:11338 clostridial tetanus, Tetanus (disorder), Infection due to Clostridium tetani (disorder)
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