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- W2518571462 abstract "The diversity of α-glucosidase was discussed from the viewpoint of substrate specificity. The substrate specificities of α-glucosidases from various origins were compared with one another on the hydrolysis velocity of α-glucosidic bond, calculated, from Vmax for the hydrolysis of substrate. It seems that many of α-glucosidases can be divided into the following three types of their substrate specificities, except an enzyme such as honey bee α-glucosidase having unusual properties. The first group (“Type I”) is the typical α-glucosidase which hydrolyzes heterogeneous substrates such as phenyl-α-glucoside and sucrose more rapidly than maltose. The second group (“Type II”) is the type of so-called maltase, showing especially high activity to homogeneous substrates such as maltooligosaccharides, but feeble or no activity to α-glucoside and sucrose. The third group (“Type III”) is characterized as α-glucosidases possessing glucoamylase activity. However, the substrate specificity of the third group may be classified into category of the second group, except that this type of a-glucosidases are capable of attacking α-glucans. The active site of α-glucosidase, like glucoamylase, was also shown to be made up by the subsite structure. The subsite affinities in the active site of buckwheat α-glucosidase, evaluated in accordance with the subsite theory, were compared with those of Rh, delemar glucoamylase. The difference in the substrate specificities between α-glucosidase and glucoamylase was interpreted on the basis of their subsite affinities." @default.
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- W2518571462 date "1978-01-01" @default.
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- W2518571462 doi "https://doi.org/10.5458/jag1972.25.105" @default.
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