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Literature summary for 3.4.24.68 extracted from
- Surface topography of histidine residues of tetanus toxin probed by immobilized-metal-ion affinity chromatography (1992), Biochem. J., 285, 9-12.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zinc | zinc-dependent endoproteinase | Clostridium tetani |  |
| Zinc | toxin surface topography of His-residues | Clostridium tetani | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium tetani | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Clostridium tetani |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP) | structure and mechanism | Clostridium tetani |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Synaptobrevin + H2O | - |
Clostridium tetani | Hydrolyzed synaptobrevin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme consists of a heavy (H) chain and a light (L) chain | Clostridium tetani |
| More | held together by a single disulfide bond and non-covalent forces | Clostridium tetani |
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Release 2023.1 (January 2023)
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