Activating Compound | Comment | Organism | Structure |
---|---|---|---|
tris-(2-carboxyethyl)-phosphine hydrochloride | i.e. TCEP, a non-odorous, oxygen-insensitive, non-toxic sulfhydryl reducing compound, activates proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells maximally at 1mM, protects against BoNT/B inhibition of noradrenaline release, achieving 72% of the release from un-intoxicated controls. TCEP significantly changes the conformation of BoNT/B holotoxin | Clostridium botulinum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
tris-(2-carboxyethyl)-phosphine hydrochloride | i.e. TCEP, a non-odorous, oxygen-insensitive, non-toxic sulfhydryl reducing compound, reduces proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells at higher concentrations above 4 mM, protects against BoNT/B inhibition of noradrenaline release, achieving 72% of the release from un-intoxicated controls. TCEP significantly changes the conformation of BoNT/B holotoxin. But TCEP does not fragment un-nicked BoNT/B holotoxin | Clostridium botulinum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc-dependent endopeptidase | Clostridium botulinum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
VAMP2 + H2O | Clostridium botulinum | i.e. synaptobrevin-2 or vesicle-associated membrane protein 2 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium botulinum | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | assay method measuring noradrenaline release in human neuronal SHSY-5Y cells | Clostridium botulinum | ? | - |
? | |
VAMP2 + H2O | i.e. synaptobrevin-2 or vesicle-associated membrane protein 2 | Clostridium botulinum | ? | - |
? | |
VAMP2 + H2O | i.e. vesicle-associated membrane protein 2 or synaptobrevin-2, with BoNT/B light chain. BoNT/B HT exhibits little ability to cleave its substrate VAMP-2, when its LC and HC subunits are held together by a disulfide bond | Clostridium botulinum | ? | - |
? | |
VAMPTide + H2O | a VAMP-2-derived peptide substrate, modified with FRET, with BoNT/B light chain | Clostridium botulinum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the BoNT HC-LC subunits are held together by a single disulfide bond | Clostridium botulinum |
Synonyms | Comment | Organism |
---|---|---|
BoNT/B | - |
Clostridium botulinum |
botulinum neurotoxin B | - |
Clostridium botulinum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Clostridium botulinum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Clostridium botulinum |
General Information | Comment | Organism |
---|---|---|
additional information | the catalytic light chain, LC, of botulinum neurotoxin B is unable to enter target neuronal cells by itself. It is brought into the cell, human neuronal SHSY-5Y cells, in association with the BoNT/B heavy chain, HC, through endocytosis | Clostridium botulinum |