EC 18.104.22.168 - Tentoxilysin
IntEnz Enzyme Nomenclature
- Hydrolysis of -Gln76┼Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP).
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
A zinc-protease specific domain in botulinum and tetanus neurotoxins.Microbiol. Intern. 36: 213-220 (1992).
Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin.Nature 359: 832-834 (1992). [PMID: 1331807]
Botulinum neurotoxins are zinc proteins.J. Biol. Chem. 267: 23479-23483 (1992). [PMID: 1429690]
Mechanism of action of tetanus and botulinum neurotoxins.Mol. Microbiol. 8: 1-13 (1994). [PMID: 7527117]
Tetanus and botulism neurotoxins.Methods Enzymol. 248: 643-652 (1995). [PMID: 7674951]
[EC 22.214.171.124 created 1995]