Schiavo G, Rossetto O, Catsicas S, Polverino de Laureto P, DasGupta B R, Benfenati F, Montecucco C
Centro Consiglio Nazionale delle Ricerche Biomembrane, Università di Padova, Italy.
J Biol Chem. 1993 Nov 15;268(32):23784-7.
Botulinum neurotoxins are metalloproteins with one zinc atom bound to the zinc binding motif of zinc endopeptidases. Here we show that botulinum neurotoxin serotypes A, D, and E are zinc endoproteases specific for components of the synaptic vesicle docking and fusion complex. Serotypes A and E cleave SNAP-25, a 25-kDa protein of the synaptic terminal, while serotype D is specific for VAMP/synaptobrevin, a membrane protein of synaptic vesicles. Both rat brain VAMP isoforms are cleaved at a single Lys-Leu peptide bond. The proteolytic activity of these neurotoxins is inhibited by EDTA and captopril.
肉毒杆菌神经毒素是金属蛋白，其中一个锌原子与锌内肽酶的锌结合基序结合。在此我们表明，A型、D型和E型肉毒杆菌神经毒素是针对突触小泡对接和融合复合物成分的锌内蛋白酶。A型和E型毒素切割SNAP-25，一种突触末端的25 kDa蛋白质，而D型毒素对VAMP/突触融合蛋白具有特异性，VAMP/突触融合蛋白是突触小泡的一种膜蛋白。大鼠脑内的两种VAMP同工型均在单个赖氨酸-亮氨酸肽键处被切割。这些神经毒素的蛋白水解活性受到EDTA和卡托普利的抑制。
