White W J, Schray K J, Legler G, Alhadeff J A
Biochim Biophys Acta. 1986 Sep 26;873(2):198-203. doi: 10.1016/0167-4838(86)90046-4.
Conduritol C trans-epoxide was found to inactivate human liver alpha-L-fucosidase (alpha-L-fucoside fucohydrolase, EC 3.2.1.51), exhibiting an apparent dissociation constant of 43 mM. The cis-isomer of the inactivator had no apparent effect on the enzyme's activity. The pH profile for the inactivation yielded two apparent pK values of approx. 3.7 and 6.1 alpha-L-Fucose (a competitive inhibitor) was effective in protecting the enzyme from inactivation. These results are consistent with a requirement for two amino acid side chains at the active site involved in the reaction of the enzyme with conduritol C trans-epoxide.
发现conduritol C反式环氧化物可使人类肝脏α-L-岩藻糖苷酶（α-L-岩藻糖苷岩藻糖水解酶，EC 3.2.1.51）失活，其表观解离常数为43 mM。失活剂的顺式异构体对该酶的活性无明显影响。失活反应的pH曲线产生了两个表观pK值，约为3.7和6.1。α-L-岩藻糖（一种竞争性抑制剂）可有效保护该酶不被失活。这些结果与在酶与conduritol C反式环氧化物反应的活性位点上需要两个氨基酸侧链的情况一致。
