Molecular Classification
Glycoside hydrolase family, Primary structure family
Other Names
acid alpha-glucosidase
Disease Roles
Pompe disease (caused by mutations in the GAA gene leading to acid alpha-glucosidase deficiency, resulting in glycogen accumulation and damage to organs, particularly muscles and heart)

Alpha-glucosidase Overview

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.

Mechanism of Action

Inhibits alpha-glucosidase enzyme activity, decreasing complex carbohydrate catabolism and retarding the rise in postprandial blood glucose levels.

Biological Functions

Carbohydrate digestion (hydrolyzing (1→4) bonds in starch and disaccharides in the small intestine)
Glycogen metabolism (lysosomal breakdown of glycogen)
Energy regulation (metabolic response to energy demands)
Industrial applications (alcohol fermentation, sugar hydrolysis, chemical synthesis)

Disease Associations

Pompe disease (caused by mutations in the GAA gene leading to acid alpha-glucosidase deficiency, resulting in glycogen accumulation and damage to organs, particularly muscles and heart)

Safety Considerations

No safety concerns listed

Interacting Drugs

Acarbose
Miglitol
Voglibose
Quercetin
Kaempferol
Luteolin
Fisetin
Isoquercetin
Naringenin
Epigallocatechin-3-gallate (EGCG)