肝脏中一种具有广泛特异性的β-葡萄糖苷酶对天然存在的β-葡萄糖苷的水解作用。
Hydrolysis of a naturally occurring beta-glucoside by a broad-specificity beta-glucosidase from liver.
作者信息
LaMarco K L, Glew R H
出版信息
Biochem J. 1986 Jul 15;237(2):469-76. doi: 10.1042/bj2370469.
Abstract
We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-denaturation, kinetic competition studies, chromatographic properties and pH optima all argue strongly that the broad-specificity beta-glucosidase is responsible for the hydrolysis of both the non-physiological aryl glycosides and L-picein. This paper demonstrates that beta-glucosidase can catalyse the hydrolysis of a natural glycoside, and may provide a key to understanding the function of this enigmatic enzyme. A possible role in the metabolism of xenobiotic compounds is discussed.
摘要
我们从豚鼠肝脏中分离出一种功能未知的广谱β-葡萄糖苷酶，它以非生理性芳基糖苷（如4-甲基伞形酮基β-D-吡喃葡萄糖苷、对硝基苯基β-D-吡喃葡萄糖苷）作为底物。本文证明该酶可被多种天然存在的糖苷抑制，包括L-松脂素、蜀黍氰苷和格氏甙。此外，作为广谱β-葡萄糖苷酶竞争性抑制剂的L-松脂素（Ki 0.65 mM）也是该酶的底物（Km 0.63 mM；Vmax. 277,000单位/毫克）。热变性、动力学竞争研究、色谱性质和最适pH均有力表明，广谱β-葡萄糖苷酶负责非生理性芳基糖苷和L-松脂素的水解。本文证明β-葡萄糖苷酶可催化天然糖苷的水解，并可能为理解这种神秘酶的功能提供关键线索。文中还讨论了其在异源生物化合物代谢中的可能作用。
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