EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.24.68 | more |
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein |
Clostridium tetani |
? |
- |
? |
| 3.4.24.68 | more |
catalytic activity requires reduction of the single interchain disulfide bond of the neurotoxin |
Clostridium tetani |
? |
- |
? |
| 3.4.24.68 | more |
no substrates are rat or chicken |
Clostridium tetani |
? |
- |
? |
| 3.4.24.68 | more |
most powerful known natural toxin |
Clostridium tetani |
? |
- |
? |
| 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 |
Clostridium tetani |
? |
- |
? |
| 3.4.24.68 | more |
most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords |
Clostridium tetani |
? |
- |
? |
| 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 |
Clostridium tetani |
? |
- |
? |
| 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 |
Clostridium tetani |
? |
- |
? |
| 3.4.24.68 | more |
the conformational changes of the C fragment of tetanus neurotoxin (TeNTHc) resulting from disulfide bond formation reduce the ganglioside-binding activity but do not destroy its immunogenicity as a potent vaccine candidate |
Clostridium tetani |
? |
- |
? |
| 3.4.24.68 | more |
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein |
Clostridium tetani Harvard |
? |
- |
? |
