Catalytic Reaction Mechanism on α-Secondary Kinetic Isotope Effects in Hydrolytic Cleavage of α-Glucosidic Linkage by α-Glycosidases

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  • IGAKI Shigeru
    Department of Applied Bioscience, Faculty of Agriculture, Hokkaido University
  • KIMURA Atsuo
    Department of Applied Bioscience, Faculty of Agriculture, Hokkaido University
  • CHIBA Seiya
    Department of Applied Bioscience, Faculty of Agriculture, Hokkaido University

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  • α一グルコシド結合の加水分解反応の際に認められたα一第二次同位体効果により推察されるα一グルコシダーゼの反応機構
  • α-グルコシド結合の加水分解反応の際に認められたα-第二次同位体効果により推察されるα-グルコシダーゼの反応機構
  • Catalytic Reaction Mechanism on アルファーSe

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α-Secondary deuterium kinetic isotope effects were investigated in the hydrolysis of [1, 1'.2H]-isomaltose with Aspergillus niger α-glucosidase, suger beet a-glucosidase, honeybee a-glucosidase II, and Paecilomyces sp. glucoamylase. The ratios kH/kD of the molecular activities in the hydrolysis of an ordinary isomaltose and the [1, 1'-2H] isomaltose enzymatically synthesized were 1.16, 1.21, 1.13, and 1.23 for α-glucosidases from A. niger, sugar beet seeds, and honeybees, and glucoamylase from Paecilomyces sp., respectively. The data strongly support the occurrence of the oxocarbenium ion intermediate in the transition states of the hydrolytic reactions by the glycosidases.

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