Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity

Matthew Wictome, Ornella Rossetto, Cesare Montecucco, Clifford Shone*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    34 Citations (Scopus)

    Abstract

    Clostridium botulinum type B neurotoxin is a highly specific zinc-endopeptidase which cleaves vesicle-associated membrane protein (VAMP/synaptobrevin), a critical component of the vesicle docking/fusion mechanism. In this study, substrate residues flanking the N-terminal side of the cleavage site are shown to play a key role in enzyme substrate recognition. Two aspartate residues in this region are identified as critical determinants of the neurotoxin's specificity. These findings are discussed in relation to the mechanism by which botulinum type B neurotoxin cleaves its substrate.

    Original languageEnglish
    Pages (from-to)133-136
    Number of pages4
    JournalFEBS Letters
    Volume386
    Issue number2-3
    DOIs
    Publication statusPublished - 20 May 1996

    Keywords

    • Botulinum
    • Neurotoxin
    • Peptide substrate
    • Synaptobrevin
    • VAMP
    • Zinc-endopeptidase

    Fingerprint

    Dive into the research topics of 'Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity'. Together they form a unique fingerprint.

    Cite this