Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Proteases | activation by rapid cleavage within an exposed loop of the single inactive MW 150000 polypeptide chain and generation of active di-chain neurotoxin | Clostridium tetani | |
Proteases | or tissue proteases | Clostridium tetani | |
Proteases | bacterial | Clostridium tetani |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
captopril | - |
Clostridium tetani |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | accumulates until bacterial lysis | Clostridium tetani | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cobalt | zinc-dependent endoproteinase, can replace zinc | Clostridium tetani | |
Nickel | zinc-dependent endoproteinase, can replace zinc | Clostridium tetani | |
Zinc | zinc-dependent endoproteinase | Clostridium tetani | |
Zinc | 1 atom zinc per molecule toxin, zinc-binding motif: His-Glu-X-X-His, nickel or cobalt can replace zinc | Clostridium tetani |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
synaptobrevin + H2O | Clostridium tetani | 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 | ? | - |
? | |
synaptobrevin + H2O | Clostridium tetani | i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol | ? | - |
? | |
synaptobrevin + H2O | Clostridium tetani | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium tetani | - |
all toxigenic strains synthesize only one type of neurotoxin | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP) | structure and mechanism | Clostridium tetani |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
in neurotoxin-injected Aplysia neurons 4-10 molecules of L-chains are sufficient to cause blockade of neurotransmitter release with a t1/2 of 20-40 min at 20°C | Clostridium tetani |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein | Clostridium tetani | ? | - |
? | |
additional information | no substrates are rat or chicken | Clostridium tetani | ? | - |
? | |
Synaptobrevin + H2O | i.e. VAMP, neuronal vesicle-associated membrane protein, MW 19000, with 2 isoforms in human, chicken, in rat brain: synaptobrevin/VAMP-1 and synaptobrevin/VAMP-2, cleaves at Gln76-Phe77, the same site as botulin neurotoxin B | Clostridium tetani | Hydrolyzed synaptobrevin | - |
? | |
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 | Clostridium tetani | ? | - |
? | |
synaptobrevin + H2O | i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol | Clostridium tetani | ? | - |
? | |
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 | Clostridium tetani | ? | - |
? |