Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Proteases | activation by rapid cleavage of MW 150000 polypeptide chain and generation of active di-chain neurotoxin | Clostridium sp. | |
Proteases | activation by rapid cleavage of MW 150000 polypeptide chain and generation of active di-chain neurotoxin | Clostridium botulinum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | accumulates until bacterial lysis | Clostridium sp. | 5829 | - |
cytosol | accumulates until bacterial lysis | Clostridium botulinum | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zinc | the L-chain of BoNT/B is a form of zinc-endopeptidase | Clostridium sp. | |
Zinc | the L-chain of BoNT/B is a form of zinc-endopeptidase | Clostridium botulinum | |
Zinc | 0.8-1 gatom zinc/mol neurotoxin | Clostridium sp. | |
Zinc | 0.8-1 gatom zinc/mol neurotoxin | Clostridium botulinum | |
Zinc | zinc-dependent endopeptidase (serotype BoNT/B) | Clostridium sp. | |
Zinc | zinc-dependent endopeptidase (serotype BoNT/B) | Clostridium botulinum | |
Zinc | atom absorption spectroscopy | Clostridium sp. | |
Zinc | atom absorption spectroscopy | Clostridium botulinum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Neuroexocytosis multi-subunit complex + H2O | Clostridium sp. | neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | Clostridium botulinum | neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | Clostridium sp. | causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | Clostridium botulinum | causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding | ? | - |
? | |
synaptobrevin + H2O | Clostridium sp. | i.e. VAMP | ? | - |
? | |
synaptobrevin + H2O | Clostridium botulinum | i.e. VAMP | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium botulinum | - |
7 serologically different neurotoxin types: BoNT/A-G | - |
Clostridium sp. | - |
- |
- |
Oxidation Stability | Organism |
---|---|
extremely sensitive to oxidants | Clostridium botulinum |
Purification (Comment) | Organism |
---|---|
serotypes BoNT/A, B, E, C, D, F | Clostridium botulinum |
Storage Stability | Organism |
---|---|
-80°C, in 10 mM HEPES buffer, pH 7.2, 50 mM NaCl, after freezing in liquid N2, stable | Clostridium botulinum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins | Clostridium sp. | ? | - |
? | |
additional information | no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins | Clostridium botulinum | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature | Clostridium sp. | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature | Clostridium botulinum | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding | Clostridium sp. | ? | - |
? | |
Neuroexocytosis multi-subunit complex + H2O | causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding | Clostridium botulinum | ? | - |
? | |
Proteins of neuroexocytosis apparatus + H2O | - |
Clostridium sp. | ? | - |
? | |
Proteins of neuroexocytosis apparatus + H2O | - |
Clostridium botulinum | ? | - |
? | |
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 sp. | Hydrolyzed synaptobrevin | - |
? | |
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 botulinum | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | hydrolyzed by serotypes BoNT/B | Clostridium sp. | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | hydrolyzed by serotypes BoNT/B | Clostridium botulinum | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | hydrolyzed by serotypes D, F or G | Clostridium sp. | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | hydrolyzed by serotypes D, F or G | Clostridium botulinum | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | carrying synaptobrevin/VAMP-2 | Clostridium sp. | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | carrying synaptobrevin/VAMP-2 | Clostridium botulinum | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | highly specific neurotoxins | Clostridium sp. | Hydrolyzed synaptobrevin | - |
? | |
Synaptobrevin + H2O | highly specific neurotoxins | Clostridium botulinum | Hydrolyzed synaptobrevin | - |
? | |
synaptobrevin + H2O | i.e. VAMP | Clostridium sp. | ? | - |
? | |
synaptobrevin + H2O | i.e. VAMP | Clostridium botulinum | ? | - |
? | |
Synaptosome-associated protein + H2O | serotype BoNT/A and E | Clostridium sp. | Hydrolyzed synaptosome-associated protein | - |
? | |
Synaptosome-associated protein + H2O | serotype BoNT/A and E | Clostridium botulinum | Hydrolyzed synaptosome-associated protein | - |
? | |
Syntaxin + H2O | serotype BoNT/C | Clostridium sp. | ? | - |
? | |
Syntaxin + H2O | serotype BoNT/C | Clostridium botulinum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds | Clostridium sp. |
More | synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds | Clostridium botulinum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Clostridium sp. |
37 | - |
assay at | Clostridium botulinum |