Firsov L M
Biokhimiia. 1978 Dec;43(12):2222-32.
Anomerities of products were estimated for glucosidases from cattle liver and Aspergillus awamori. It was demonstrated that the enzyme from cattle liver is alpha-glucosidase and that from Asp. awamori is exogluconase. It was demonstrated that alpha-glucosidase hydrolyzes the C1--O bond in the course of reaction. delta-Lactone of gluconic acid is a competitive inhibitor for both enzymes. The secondary kinetic isotope effects for both enzymes were measured. The isotope effect for alpha-glucosidase is equal to 1, for exogluconase 1,1 for glycogen and 1,18 for maltose. Some aspects of mechanisms of both enzymes are discussed in terms of the data obtained.
对牛肝和泡盛曲霉中的葡糖苷酶产物的异头物情况进行了评估。结果表明，牛肝中的酶是α-葡糖苷酶，而泡盛曲霉中的酶是外切葡糖酶。已证明α-葡糖苷酶在反应过程中水解C1--O键。葡萄糖酸δ-内酯是这两种酶的竞争性抑制剂。测定了这两种酶的二级动力学同位素效应。α-葡糖苷酶的同位素效应等于1，外切葡糖酶对糖原的同位素效应为1.1，对麦芽糖的同位素效应为1.18。根据所获得的数据讨论了这两种酶机制的一些方面。
