Final answer:
Glycogen remodeled by transferase and α-1,6-glucosidase allows for further phosphorolysis by glycogen phosphorylase, an enzyme which releases glucose units from non-reducing ends of glycogen until branching points limit its action.
Step-by-step explanation:
When glycogen is remodeled by transferase and α-1,6-glucosidase debranching enzyme, it creates longer free ends which enables further phosphorolysis by glycogen phosphorylase. This enzyme is crucial for glycogen breakdown, as it acts only on α-1→ 4 glycosidic linkages, releasing glucose units from the linear chain until it reaches the branching points. At this position, the remaining glucose units linked by α-1→ 4 linkages are transferred to another linear chain by glucan transferase and the single glucose residue linked by an α-1→ 6 linkage is released by amylo-1,6-glycosidase, leaving a non-reducing end available for further action by glycogen phosphorylase.
Glycogen phosphorylase continues glycogenolysis by cleaving off glucose-1-phosphate molecules from the non-reducing ends of the glycogen molecule. This process of sequential removal of glucose units is essential for the production of free glucose, especially during fight-or-flight responses where rapid glucose mobilization is required.