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Literature summary for 3.4.24.69 extracted from
- Catalytic properties of botulinum neurotoxin subtypes A3 and A4 (2009), Biochemistry, 48, 2522-2528.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | BoNTs are among the most useful reagents to treat neuromuscular afflictions | Clostridium botulinum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His6-tagged light chains of thr BoNT subtypes in Escherichia coli | Clostridium botulinum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics, overview | Clostridium botulinum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | the C-terminal B domain, i.e. heavy chain, HC, is composed of two functional domains that are involved in receptor recognition and translocation of the light chain across the host cell endosomal membrane | Clostridium botulinum | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | the N-terminal A domain, i.e. light chain, LC, is a 50 kDa zinc metalloprotease with the characteristic thermolysin-family zinc coordination motif HExxH | Clostridium botulinum |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium botulinum | - |
BoNT/A1, BoNT/A2, BoNT/A3, and BoNT/A4 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged light chains of the BoNT subtypes from Escherichia coli by nickel affinity chromatography | Clostridium botulinum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | substrate specificities of the BoNT light chain subtypes, overview. The LC subtypes perform autolytic cleavage. Each LC/A subtype possesses the di-tyrosine autocleavage site, which indicate that residues in addition to the cleavage site are necessary for autocleavage. Control LC, LC/A1 DYM, contains mutations to cleavage site residues, Y250A and Y251A, which abrogates autocatalysis in LC/A1 | Clostridium botulinum | ? | - |
? | |
| SNAP-25 + H2O | i.e. 25-kDa synaptosome-associated protein, substrate of light chains of BoNT/A1, BoNT/A2, BoNT/A3, and BoNT/A4 | Clostridium botulinum | ? | - |
? | |
| SNAP-25-derived peptide + H2O | i.e. HA-tagged SNAP25(141-206) or HA-tagged mutant SNAP25(141-206)-R198A, substrate of light chains of BoNT/A1, BoNT/A2, BoNT/A3, and BoNT/A4 | Clostridium botulinum | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BoNT | - |
Clostridium botulinum |
| BoNT/A1 | - |
Clostridium botulinum |
| BoNT/A2 | - |
Clostridium botulinum |
| BoNT/A3 | - |
Clostridium botulinum |
| BoNT/A4 | - |
Clostridium botulinum |
| botulinum neurotoxin subtype A3 | - |
Clostridium botulinum |
| botulinum neurotoxin subtype A4 | - |
Clostridium botulinum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Clostridium botulinum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Clostridium botulinum |
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