Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | design, random selection, and recombinant production from phagemid in Escherichia coli of human single chain antibody fragments that inhibit tetanus toxin binding to retinoic acid pulsed human neuroblastoma cells and TeNT protease activity completely, overview | Clostridium tetani |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | dependent on | Clostridium tetani |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
synaptobrevin + H2O | Clostridium tetani | TeNT is a zinc metalloprotease, that is produced by anaerobically grown Clostridium tetani in infected tissue, where it binds to ganglioside receptors of peripheral nerves. TeNT is then endocytosed. The A subunit exits from the endosome and undergoes retrograde transport via the nerve axon to the spinal cord of the host, where it specifically cleaves one of the nerve cell SNARE proteins, synaptobrevin | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium tetani | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
synaptobrevin + H2O | TeNT is a zinc metalloprotease, that is produced by anaerobically grown Clostridium tetani in infected tissue, where it binds to ganglioside receptors of peripheral nerves. TeNT is then endocytosed. The A subunit exits from the endosome and undergoes retrograde transport via the nerve axon to the spinal cord of the host, where it specifically cleaves one of the nerve cell SNARE proteins, synaptobrevin | Clostridium tetani | ? | - |
? | |
synaptobrevin + H2O | a host nerve cell SNARE protein, purified recombinant His-tagged synaptobrevin expressed in Escherichia coli | Clostridium tetani | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | TeNT is an A-B toxin. It consits of a heavy chain containing cellular receptor binding domain and a light chain with zinc metalloprotease activity | Clostridium tetani |
Synonyms | Comment | Organism |
---|---|---|
TeNT | - |
Clostridium tetani |
tetanospasmin | - |
Clostridium tetani |
Tetanus neurotoxin | - |
Clostridium tetani |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Clostridium tetani |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Clostridium tetani |
General Information | Comment | Organism |
---|---|---|
physiological function | cleavage of synaptobrevin results in inhibition of release of neurotransmitters glycine and gamma-amino butyric acid from inhibitory interneurons causing spastic paralysis | Clostridium tetani |