Any feedback?
Literature summary for 3.4.24.69 extracted from
- Novel chimeras of botulinum neurotoxin /A and /E unveil contributions from the binding, translocation and protease domains to their functional characteristics (2008), J. Biol. Chem., 283, 16993-17002.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DTT | near-complete conversion of the enzyme SC to a disulfide-linked DC in the presence of DTT | Clostridium botulinum |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged BoNT AE and EA chimeras in Escherichia coli strain BL21 | Clostridium botulinum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of BoNT AE and EA chimeras from serotypes BoNT/A and BoNT/E in DC and SC forms, overview, catalytic and physiological properties of the chimeric forms, overview | Clostridium botulinum |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | - |
Clostridium botulinum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 146000 | - |
recombinant His-tagged BoNT AE and EA chimeras, gel filtration | Clostridium botulinum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Clostridium botulinum | the seven serotypes A-G potently block neurotransmission by binding to presynaptic receptors, undergoing endocytosis, transferring to the cytosol, and inactivating proteins essential for vesicle fusion, overview | ? | - |
? | |
| SNAP-25 + H2O | Clostridium botulinum | serotypes BoNT/A and BoNT/E cleave SNAP-25 at distinct sites, BoNT/E blocks neurotransmission faster and more potently | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium botulinum | Q00496 | seven BoNT serotypes A-G | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged BoNT AE and EA chimeras from Escherichia coli strain BL21 by immobilized metal affinity and adsorption chromatography, followed by gel filtration, to homogeneity, near-complete conversion of the SC to a disulfide-linked DC as revealed by the appearance of the HC and LC upon SDS-PAGE in the presence of DTT | Clostridium botulinum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the seven serotypes A-G potently block neurotransmission by binding to presynaptic receptors, undergoing endocytosis, transferring to the cytosol, and inactivating proteins essential for vesicle fusion, overview | Clostridium botulinum | ? | - |
? | |
| SNAP-25 + H2O | serotypes BoNT/A and BoNT/E cleave SNAP-25 at distinct sites, BoNT/E blocks neurotransmission faster and more potently | Clostridium botulinum | ? | - |
? | |
| SNAP-25 + H2O | substrate is a recombinant GFP-SNAP-25-(134206)-His6 fusion protein | Clostridium botulinum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 146000, recombinant His-tagged BoNT AE and EA chimeras, SDS-PAGE | Clostridium botulinum |
| More | near-complete conversion of the SC to a disulfide-linked DCas revealed by the appearance of the HC and LC upon SDS-PAGE in the presence of DTT | Clostridium botulinum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BoNT | - |
Clostridium botulinum |
| botulinum toxin | - |
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 |
|---|---|---|---|
| 7.4 | - |
assay at | Clostridium botulinum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
