Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Botulinum Toxins / metabolism*
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Cerebral Cortex / metabolism
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Kinetics
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Membrane Proteins / metabolism*
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Metalloendopeptidases / metabolism*
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Molecular Sequence Data
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Molecular Weight
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Nerve Tissue Proteins / metabolism*
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Neurotoxins / metabolism*
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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R-SNARE Proteins
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Rats
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Sequence Homology, Amino Acid
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Spectrophotometry, Atomic
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Substrate Specificity
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Synaptic Vesicles / metabolism
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Trace Elements / analysis
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Zinc / analysis*
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Zinc / pharmacology
Substances
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Membrane Proteins
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Nerve Tissue Proteins
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Neurotoxins
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Peptide Fragments
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R-SNARE Proteins
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Trace Elements
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Metalloendopeptidases
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Botulinum Toxins
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Zinc