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Literature summary for 3.4.24.69 extracted from
- Neuronal targeting, internalization, and biological activity of a recombinant atoxic derivative of botulinum neurotoxin A (2011), Biochem. Biophys. Res. Commun., 405, 673-677.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | an atoxic derivative of BoNT/A (BoNT/A ad) as a full-length 150 kDa molecule consisting of a 50 kDa light chain and a 100 kDa heavy chain joined by a disulfide bond and metalloprotease-inactivating point mutations (E224A/Y366A) in the light chain. Studies in neuronal cultures demonstrates that the mutant is unable to cleave SNAP25, and that it effectively competes with wild-type BoNT/A for binding to endogenous neuronal receptors. In vivo studies indicate accumulation of the mutant (BoNT/A ad) at the neuromuscular junction of the mouse diaphragm. Toxicity of the mutant BoNT/A ad is reduced by 100000fold relative to wild-type BoNT/A | Clostridium botulinum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium botulinum | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BoNT/A | - |
Clostridium botulinum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Clostridium botulinum |
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Release 2023.1 (January 2023)
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