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Literature summary for 3.4.24.69 extracted from
- Molecular basis of activation of endopeptidase activity of botulinum neurotoxin type E (2010), Biochemistry, 49, 2510-2519.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | nicking of the single chain BoNT/E to the dichain form is associated with 100fold increase in toxicity, activation mechanism of botulinum neurotoxin type E upon nicking and subsequent reduction of disulfide bond, overview | Clostridium botulinum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 25-kDa synaptosome-associated protein + H2O | Clostridium botulinum | i.e. SNAP-25 | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium botulinum | - |
various strains, seven serotypes BoNT A-G | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | BoNTs are synthesized as single inactive polypeptide chains that are cleaved by endogenous or exogenous proteases to generate the active dichain form of the toxin. Nicking of the single chain BoNT/E to the dichain form is associated with 100fold increase in toxicity | Clostridium botulinum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 25-kDa synaptosome-associated protein + H2O | i.e. SNAP-25 | Clostridium botulinum | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BoNT/E | - |
Clostridium botulinum |
| botulinum neurotoxin type E | - |
Clostridium botulinum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Clostridium botulinum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 50 | 20% of maximal activity at 20°C, as the temperature is increased to 45°C, the endopeptidase activity dramatically decreases to 21% cleavage of SNAP-25, but at 50°C its enzymatic activity increases again to 64% cleavage of SNAP-25, 4% of maximal activity at 60°C | Clostridium botulinum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermodynamic parameters for temperature-induced denaturation of BoNT/E, overview | Clostridium botulinum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Clostridium botulinum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | BoNT acts on the host neuromuscular junction by blocking the release of the neurotransmitter acetylcholine, thereby resulting in flaccid muscle paralysis | Clostridium botulinum |
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