Amylo-α-1,6-glucosidase Overview
Amylo-α-1,6-glucosidase is a hydrolase enzyme (EC 3.2.1.33) that specifically catalyzes the hydrolysis of α-1,6 branch linkages in glycogen phosphorylase-limit dextrin, a critical step in glycogen breakdown. This activity is an integral part of the glycogen debranching system, particularly in mammals, where the enzyme is coupled with transferase activity in a single polypeptide called glycogen debranching enzyme[2][6]. Deficiency of this enzymatic function results in abnormal glycogen metabolism, manifesting clinically as Cori disease (Glycogen Storage Disease type III)[5][6]. The enzyme is important for releasing glucose from branched glycogen during times of energy demand. There is no evidence of incorrectness in the target name, but confusion may arise as α-glucosidase (EC 3.2.1.20) is a more general term for enzymes hydrolyzing α-1,4-linkages, while amylo-α-1,6-glucosidase is responsible for α-1,6-branch hydrolysis specifically[6][2].
Mechanism of Action
Substrate hydrolysis (enzymatic cleavage of α-1,6 glycosidic bonds in glycogen limit dextrins)
Biological Functions
Disease Associations
Safety Considerations
- Therapeutic challenges mainly concern enzyme deficiency causing disease; enzyme replacement therapies for related but distinct enzymes may have immunogenicity or infusion reactions[5].
- No direct small-molecule inhibitors are currently in use for this specific enzyme; off-target effects would be theoretical.
Interacting Drugs
Associated Biomarkers
Biomarker |
---|
Enzyme activity assays for debranching enzyme function (used in diagnostic panels for glycogen storage diseases) |