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J. Biochem, 1990, Vol. 108, No. 1 42-46
© 1990 Japanese Biochemical Society

research-article

Inhibitory Effect of Pseudo-Aminosugars on Oligosaccharide Glucosidases I and II and on Lysosomal {alpha}-Glucosidase from Rat Liver

Masayoshi Takeuchi1, Kanae Kamata, Masahiro Yoshida, Yukihiko Kameda and Katsuhiko Matsui2

Department of Biochemistry, School of Pharmacy, Hokuriku University Kanazawa, Ishikawa 920-11
1Present address: Fuji Chemical Industries, Ltd., 530 Chokeiji, Takaoka, Toyama 933.

2To whom correspondence should be addressed

We examined the inhibitory effect of three pseudo-aminosugars (validamine, valienamine, and valiolamine), which were isolated from the broth of Streptomyces hygroscopicus, on the oligosaccharide-processing glucosidases I and II involved in glycoprotein biosynthesis in rat liver. Both glucosidases I and II were inhibited to the same extent by the pseudo-aminosugars, and valiolamine had a more potent inhibitory activity than validamine or valienamine. A 50% inhibition of valiolamine was observed at 12 µM for glucosidase I and glucosidase II activities acting respectively on the substrates Glc3Man9GlcNAc2 and p-nitrophenyl {alpha}-D-glucopyranoside. Further, in order to investigate further the ability of valiolamine to inhibit glucosidase I, reaction products were analyzed by gel nitration on a Bio-Gel P-4 column. We also compared the inhibitory action of these pseudo-aminosugars on the acid {alpha}-glucosidase of rat liver lysosomes. They competitively inhibited the hydrolysis of both substrates, maltose and glycogen. Valiolamine again had a more potent lysosomal {alpha}-glucosidase inhibitory activity than the other two. The K1 values of valiolamine for the hydrolysis of maltose and glycogen were 8.1 and 11 µM, respectively. Valiolamine is a particularly effective inhibitor of oligosaccharide glucosidases I and II and of lysosomal {alpha}-glucosidase. Hence valiolamine might be useful as a research tool in investigations of carbohydrate metabolism.


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