| amylo-1,6-glucosidase | <enzyme> Catalyses endohydrolysis of 1,6-alpha-d-glucoside linkages at points of branching in chains of 1,4-linked alpha-d-glucose residues Registry number: EC 3.2.1.33 (26 Jun 1999) |
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| amylo-1,6-glucosidase |
[EC 3.2.1.33] an enzyme of the hydrolase class that catalyzes the cleavage of terminal α-1,6-glucoside linkages, releasing free glucose residues. In mammals, the enzyme also has a transferase activity on the same polypeptide chain (see oligo-1,4-1,4-glucantransferase) and can hydrolyze such linkages occurring at points of branching in glycogen molecules by first transferring to nearby chains those triglucosides adjacent to branch points, thereby exposing the α-1,6-linked branch points to the glucosidase activity. In concert with glycogen phosphorylase, the enzyme can thus degrade glycogen to free glucose and glucose 1-phosphate. It is found in liver and muscle. Deficiency of the enzyme, an autosomal recessive trait, results in glycogen storage disease type III. Called also debranching enzyme (of glycogen).
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