Maltase-glucoamylase, intestinal (MGAM)

Maltase-glucoamylase, intestinal is a membrane-bound alpha-glucosidase enzyme encoded by the MGAM gene, located on human chromosome 7q34[1][4][9]. It is expressed on the brush border of the small intestinal epithelium and is essential for the final steps of starch digestion, hydrolyzing alpha-1,4-glycosidic linkages of oligosaccharides and disaccharides to release glucose[1][2][6][7]. The enzyme has two homologous catalytic subunits (N-terminal and C-terminal), each with different substrate specificities, allowing efficient digestion of a broad range of dietary starches[1][2][5]. MGAM works in concert with sucrase-isomaltase, and together they permit effective utilization of plant-derived starch as a dietary carbohydrate source[1][5][9]. MGAM is the molecular target of alpha-glucosidase inhibitor drugs used to treat postprandial hyperglycemia in diabetes by slowing intestinal glucose absorption[4][2]. Deficiencies or inhibition of MGAM can contribute to malabsorption and gastrointestinal symptoms.

Other names

glucan 1,4-alpha-glycosidasemaltase-glucoamylase (alpha-glucosidase)MGA

Inhibition of intestinal maltase-glucoamylase to delay hydrolysis of starch into glucose, blunting postprandial hyperglycemia[2][4]