Schiavo G, Shone C C, Rossetto O, Alexander F C, Montecucco C
Centro Consiglio Nazionale delle Ricerche Biomembrane, Università di Padova, Italy.
J Biol Chem. 1993 Jun 5;268(16):11516-9.
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.
F型肉毒杆菌神经毒素含有锌内肽酶的锌结合基序。对高度纯化的毒素制剂进行原子吸收分析表明,每分子毒素含有一个锌原子,该锌原子可用乙二胺四乙酸(EDTA)或邻菲罗啉去除。神经毒素的轻链显示出对VAMP/突触小泡蛋白(一种突触小泡的整合膜蛋白)具有锌依赖性蛋白酶活性。大鼠VAMP的两种同工型在与其序列中存在的单个谷氨酰胺-赖氨酸肽键相对应的相同位点被切割。这种蛋白水解活性受到EDTA、邻菲罗啉、卡托普利以及跨越切割位点的VAMP肽的抑制。