Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin
| Autor: | C. C. Shone, Giampietro Schiavo, Ornella Rossetto, Cesare Montecucco, F. C. G. Alexander |
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| Rok vydání: | 1993 |
| Předmět: |
Botulinum Toxins
Synaptobrevin medicine.medical_treatment Molecular Sequence Data Neurotoxins chemistry.chemical_element Nerve Tissue Proteins Zinc medicine.disease_cause Biochemistry Synaptic vesicle Substrate Specificity R-SNARE Proteins medicine Neurotoxin Animals Amino Acid Sequence Molecular Biology Integral membrane protein Cerebral Cortex Protease Binding Sites Sequence Homology Amino Acid Chemistry Spectrophotometry Atomic Membrane Proteins Metalloendopeptidases Cell Biology Molecular biology Endopeptidase Peptide Fragments Rats Trace Elements Molecular Weight Kinetics Clostridium botulinum Synaptic Vesicles |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0021-9258 |
| Popis: | Botulinum neurotoxin serotype F contains the zinc binding motif of zinc endopeptidases. Atomic adsorption analysis of highly purified toxin preparation revealed the presence of one atom of zinc per molecule of toxin, which could be removed with EDTA or o-phenanthroline. The light chain of the neurotoxin was shown to have a zinc-dependent protease activity specific for VAMP/synaptobrevin, an integral membrane protein of synaptic vesicles. Both isoforms of rat VAMP were cleaved at the same site corresponding to the single Gln-Lys peptide bond present in their sequences. This proteolytic activity was inhibited by EDTA, o-phenanthroline, and captopril as well as by VAMP peptides spanning the cleavage site. |
| Databáze: | OpenAIRE |
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