Glucosidase

Glucosidase enzymes catalyze hydrolysis of glycosidic bonds and support carbohydrate processing in lysosomes and intestinal brush-border digestion[1][2]. Mechanistically, lysosomal acid α-glucosidase (GAA) participates in lysosomal glycogen breakdown, and GAA deficiency causes Pompe disease with glycogen accumulation and cellular damage, especially in cardiac and skeletal muscle[1]. In intestinal models, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) catalyze the final glucose-releasing step of starch digestion, making human intestinal α-glucosidases practical targets for carbohydrate digestion research[2][3]. Compared with related isoforms, MGAM and SI show overlapping but distinct substrate selectivity, while lysosomal GAA differs by cellular localization and disease linkage[1][3]. For experimental applications, acarbose inhibited human sucrase, maltase, and isomaltase activities with IC50 values of 1.65, 13.9, and 39.1 µM, respectively, in Caco-2/TC7 cell-free extracts[4]. Selective inhibitor design for lysosomal GAA can exploit an alkyl-chain storage site, and α-1-C-heptyl-LAB showed potent GAA inhibition with an IC50 of 0.44 µM and selectivity index of 168.2[5].