Other Sugar Pathways (Module 3 Lecture 1) Flashcards
What enzymes are needed for glycogenolysis?
- Glycogen phosphorylase
- Transferase
- Alpha 1,6-glycosidase
Define glycogenolysis.
Removing glucose (one by one) from glycoen via phosphorylysis NOT hydrolysis.
Describe the role of glycogen phosphorylase:
Glycogen (n residues) –> Glucose 1-phosphate + Glycogen (n - 1 residues)
Describe the role of transferase during glycogenolysis.
- After glycogen phosphorylase has reduced branches to 4 linkages,
- Transferase transfers 3 glycosyl residues to main chain
- Alpha 1,6-glycosidase releases the remaining glycosyl residue (with the 1,6 attachment) as free glucose).
Describe the conversions between glucose 1-phosphate, glucose 6-phosphate, and glucose.
- Glucose 6-phosphate is used for glycolysis in most cells.
- Liver cells convert glucose 6-phosphate into free glucose, which can leave the cell (glucose 6-phosphatase = enzyme responsible).
- Phosphoglucomutase converts glucose 1-phosphate into glucose 6-phosphate.
Describe phosphoglucomutase’s activity.
- Enzyme has serine residue in active site which reversibly binds to phosphate in glucose depending on substrate/product concentrations.
- Two steps reversible rxn: Glucose 1-phosphate glucose Glucose 6-phosphate
How is the breakdown of glycogen regulated?
By activating glycogen phosphorylase through epinephrine and glucagon, which trigger intracellular signaling cascades.
Describe the steps in activating glycogen phosphorylase.
- Epinephrine binds to external cell membrane.
- Internal cell membrane phosphorylates GDP –> GTP and dissociation of G-protein’s subunits beta and gamma
- GTP-alpha activates adenylate cyclase to make cAMP
- cAMP activates protein kinase A
- Protein kinase A activates glycogen phosphorylase kinase
- Glycogen phosphorylase kinase activates (via phosphorylation) glycogen phosphorylase.
What is one benefit of a transduction cascade for glygogenolysis?
Each enzymatic step activates multiple molecules at once, so the results are amplification.