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Alpha-glucosidase is an enzyme belonging to the glycoside hydrolase family that plays a crucial role in carbohydrate metabolism. It hydrolyzes terminal non-reducing (1→4)-linked α-glucose residues in starch and disaccharides to release single α-glucose molecules. The enzyme is widely distributed across organisms and is classified into two main families based on primary structure. Key structural elements include a TIM barrel catalytic domain (A), a loop-rich domain (B), a conserved domain C, and a distinctive β → α loop 4 related to substrate specificity. Catalytic function involves residues such as a catalytic triad (e.g., Glu202, Asp266, Glu329 in QsGH13) or Trp-516 and Asp-518 in human lysosomal α-glucosidase.
Inhibits alpha-glucosidase enzyme activity, decreasing complex carbohydrate catabolism and retarding the rise in postprandial blood glucose levels.
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