The Enzyme Database

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EC 3.4.24.68     
Accepted name: tentoxilysin
Reaction: Hydrolysis of -Gln76┼Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
Other name(s): tetanus neurotoxin
Comments: Zinc enzyme produced by Clostridium tetani. Proenzyme of 150 kDa is processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activity. Weakly inhibited by captopril, and phosphoramidon. The clostridial neurotoxins disable the neuroexocytosis apparatus, and have been described as the most toxic substances known. Tentoxilysin acts at the spinal inhibitory interneurons, blocking the release of various neurotransmitters to produce spastic paralysis. Type example of peptidase family M27 (tentoxilysin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 107231-12-9
References:
1.  Fujii, N., Kimura, K., Yashiki, T., Tsuzuki, K., Moriishi, K., Yokosawa, N., Syuto, B. and Oguma, K. A zinc-protease specific domain in botulinum and tetanus neurotoxins. Microbiol. Intern. 36 (1992) 213–220. [PMID: 1376283]
2.  Schiavo, G., Benfenati, F., Poulain, B., Rossetto, O., Polverino de Laureto, P., DasGupta, B.R. and Montecucco, C. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359 (1992) 832–834. [PMID: 1331807]
3.  Schiavo, G., Rossetto, O., Santucci, A., DasGupta, B.R. and Montecucco, C. Botulinum neurotoxins are zinc proteins. J. Biol. Chem. 267 (1992) 23479–23483. [PMID: 1429690]
4.  Montecucco, C. and Schiavo, G. Mechanism of action of tetanus and botulinum neurotoxins. Mol. Microbiol. 8 (1994) 1–13. [PMID: 7527117]
5.  Schiavo, G. and Montecucco, C. Tetanus and botulism neurotoxins. Methods Enzymol. 248 (1995) 643–652. [PMID: 7674951]
[EC 3.4.24.68 created 1995]
 
 


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