Glycogen Metabolism Notes
Glycogen Structure
- Storage form of glucose, polymer linked by α-1,4 glycosidic bonds with α-1,6 branches every 12 residues.
- Major stores in liver (10% by weight, maintains blood glucose) and muscle (2% by weight, meets energy needs).
- Exists as granules containing ~55,000 glucose molecules.
Glycogen Degradation (Glycogenolysis)
- Yields glucose 6-phosphate; requires four enzymes.
- Phosphorylase: Key enzyme, cleaves glycogen at 1,4 position via phosphorolysis (addition of orthophosphate Pi), releasing glucose 1-phosphate.
- Glycogen + Pi \leftrightarrow glucose \space 1-phosphate + glycogen \space (n-1 \space residues)
- Debranching Enzyme: Required due to α-1,6 branches.
- Transferase Activity: Shifts 3 glucosyl residues from one branch to another.
- α-1,6-Glucosidase Activity: Hydrolyzes the α-1,6 linkage.
- Phosphoglucomutase: Converts glucose 1-phosphate to glucose 6-phosphate.
- Releasing Glucose from Liver:
- Liver contains Glucose 6-phosphatase, which cleaves phosphoryl group from G-6P.
- Glucose \space 6-phosphate + H20 \rightarrow glucose + Pi
Regulation of Phosphorylase Activity
- Controlled by allosteric effectors (energy state) and reversible phosphorylation (hormones).
- Liver: Exists mostly in active a form (R state); binding of glucose shifts it to inactive T state.
- Muscle: Default state is inactive b form (T state); activated by AMP during contraction; glucose 6-phosphate stabilizes b form.
- Hormonal Control: Glucagon (low blood glucose) and adrenaline (exercise) lead to phosphorylation and activation via Protein Kinase A (PKA).
Glycogen Synthesis (Glycogenesis)
- Uses uridine diphosphate glucose (UDP-glucose) as activated glucose donor.
- Glycogenn + UDP-glucose \rightarrow glycogenn+1 + UDP
- Degradation: Glycogenn+1 + UDP + Pi \rightarrow glycogenn + glucose \space 1-phosphate
- Glycogen Synthase: Key enzyme, transfers glucose from UDP-glucose to glycogen.
- Can only add to polysaccharide with 4+ residues; requires glycogenin as a primer.
- Branching Enzyme: Creates α-1,6 linkages by transferring 7 residues to create a new branch.
- Glycogen synthase exists in active (a, non-phosphorylated) and inactive (b, phosphorylated) forms.
- PKA phosphorylates Glycogen Synthase Kinase (GSK), turning it OFF.
- Protein phosphatase 1 (PP1) reverses this process.
- Effects of Insulin:
- Stimulates glycogen production by inactivating glycogen synthase kinase.
- Insulin receptor is a tyrosine kinase; phosphorylation recruits GLUT to the cell membrane.
- PP1 dephosphorylates Glycogen Synthase (GS) to turn off the cycle.