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

FEBS Letters

Montecucco, Cesare¹  Wictome, Matthew²  Rossetto, Ornella¹  Shone, Clifford C.² 

[1] Dipartimento di Scienze Biomediche, Universita di Padova, Via Trieste 75, Padua, Italy;Centre for Applied Microbiology and Research, Porton Down, Salisbury, Wiltshire SP4 0JG, UK

关键词: Botulinum;    Neurotoxin;    VAMP;    Synaptobrevin;    Zinc-endopeptidase;    Peptide substrate;    BoNT/B;    botulinum type B neurotoxin;    VAMP;    vesicle-associated membrane protein;   

DOI  :  10.1016/0014-5793(96)00431-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown