- amylo-16-glucosidase
- am·y·lo-1,6-glu·co·si·dase (am″ə-lo-gloo-koґsĭ-dās) [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. Both liver and muscle isoforms exist; deficiency of one or both isoforms results in glycogen storage disease, type III. Called also debranching enzyme (of glycogen).
Medical dictionary. 2011.