alpha16glucosidase

Note: There is no widely recognized enzyme specifically named "alpha16glucosidase" in standard nomenclature. The closest and commonly studied enzyme is alpha-1,6-glucosidase, also known as amylo-1,6-glucosidase or part of the debranching enzyme system responsible for glycogen and starch metabolism.

Alpha-1,6-glucosidase is an enzyme that cleaves α-1,6-glycosidic bonds at branch points in branched polysaccharides such as glycogen and limit dextrins. It functions as part of a debranching system that also includes a 4-α-glucanotransferase activity; together these activities enable complete hydrolysis of branched glucose chains, allowing glycogen or starch to be further degraded into glucose units for cellular energy.

Biological role and distribution vary by organism. In humans, the glycogen debranching enzyme is encoded by the AGL gene and provides both 4-α-glucanotransferase and amylo-1,6-glucosidase activities. In plants, limit dextrinase (a related α-1,6-glucosidase) participates in starch breakdown during germination and grain utilization. Bacterial and fungal systems also harbor analogous debranching enzymes that contribute to carbohydrate metabolism.

Clinical significance: Deficiency or dysfunction of the human glycogen debranching enzyme causes glycogen storage disease type III (Cori disease), characterized by abnormal glycogen structure with limit dextrin-like accumulations, hepatomegaly, hypoglycemia, and muscle weakness. Management is supportive, focusing on maintaining normoglycemia and metabolic stability.