Donsimoni R, Legler G, Bourbouze R, Lalegerie P
Laboratoire de Biochimie, Hôpital Tenon, Paris, France.
Enzyme. 1988;39(2):78-89.
This work describes the purification of a beta-glucosidase (beta-D-glucoside-glucohydrolase EC 3.2.1.21) from the digestive juice of Helix pomatia and the study of the enzyme's active site by using different reversible and irreversible inhibitors. The catalytic constants of arylglycosides and their pH-dependent variations have also been determined. The inhibition studies demonstrate that conduritol epoxides are irreversible inhibitors of beta-glucosidase from the digestive juice of H. pomatia, and that nojirimicin shows tight binding with glucosidase: the formation and dissociation of the enzyme-inhibitor complex (dissociation constant 1.1 mumol/1) required several minutes.
这项工作描述了从苹果螺消化液中纯化一种β-葡萄糖苷酶（β-D-葡糖苷-葡萄糖水解酶，EC 3.2.1.21），并通过使用不同的可逆和不可逆抑制剂来研究该酶的活性位点。还测定了芳基糖苷的催化常数及其pH依赖性变化。抑制研究表明，己糖醇环氧化物是苹果螺消化液中β-葡萄糖苷酶的不可逆抑制剂，野尻霉素与葡糖苷酶表现出紧密结合：酶-抑制剂复合物的形成和解离（解离常数1.1 μmol/1）需要几分钟。
