Intestinal alpha-glucosidase enzyme

Intestinal alpha-glucosidase enzymes are found on the brush border of the small intestine, where they catalyze the hydrolysis of terminal, non-reducing 1→4-linked alpha-glucose residues from oligosaccharides and disaccharides, releasing free glucose that is then absorbed across the intestinal mucosa[5][4][1]. The principal human intestinal alpha-glucosidases are sucrase-isomaltase and maltase-glucoamylase, which degrade dietary starch and disaccharides (such as maltose and sucrose) during digestion[1][4][7]. Inhibition of these enzymes delays carbohydrate digestion and glucose absorption, resulting in a reduced rise in postprandial blood glucose and improved glycemic control in individuals with diabetes mellitus. The enzymes belong to the glycoside hydrolase families GH13 and GH31, and their structure is characterized by a (β/α)-barrel catalytic domain[1][3]. Alpha-glucosidase inhibitors such as acarbose, miglitol, and voglibose are approved for the management of type 2 diabetes, acting chiefly by this mechanism[4][7].

Other names

intestinal alpha-glucosidasebrush border alpha-glucosidasesucrase-isomaltasemaltase-glucoamylaseintestinal glycosidases

Competitive inhibition of carbohydrate-hydrolyzing activity (inhibition of cleavage of α-1,4 glycosidic bonds in oligosaccharides and disaccharides), leading to delayed intestinal glucose absorption and blunted postprandial blood glucose rise[4][7].