EC Number |
Natural Substrates |
---|
3.4.24.68 | more |
most powerful known natural toxin |
3.4.24.68 | more |
most powerful known natural toxin, 2 carbohdrate binding sites in the Hcc-domain of tetanus neurotoxin are required for toxicity |
3.4.24.68 | more |
most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords |
3.4.24.68 | more |
tetanus neurotoxin is a potent inhibitor of neuroexocytosis. Organization and regulation of the neurotoxin gene. The gene located immediately upstream of the tetanus toxin gene, encodes a positive regulatory protein, TetR |
3.4.24.68 | more |
TeNT high affinity binding to neurons is mediated solely by its gangliosides, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells. Gangliosides are functional dual receptors for TeNT, overview |
3.4.24.68 | synaptobrevin + H2O |
- |
3.4.24.68 | synaptobrevin + H2O |
tetanus neurotoxin receptors are located on the motor neuron plasmalemma at neuromuscular junction, after binding the toxin is internalized inside vesicles of unknown nature and then translocated across the vesicle membrane |
3.4.24.68 | synaptobrevin + H2O |
i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol |
3.4.24.68 | synaptobrevin + H2O |
enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known |
3.4.24.68 | synaptobrevin + H2O |
neurotoxin blocks neurotransmitter release in Aplysia neurons |