BIOC311 Module 2

Page 1: Glycogen Overview

  • Glycogen: Branched polymer of glucose.

  • Levels increase after meals; utilized during fasting/exercise.

  • Glycogen granules: Contain enzymes for synthesis/breakdown, up to 50,000 glucose units.

  • Purpose of Glycogen Storage:

    • Faster catabolism than fatty acids.

    • Usable under anaerobic conditions in muscles.

    • Maintains osmotic pressure.

    • Provides Glucose-1-Phosphate (G1P) faster than blood glucose uptake.

  • Tissue-Specific Roles of Glycogen:

    • Muscle: Provides local ATP for contraction (2% by weight); cannot release glucose into the blood due to absence of G6P phosphatase.

    • Liver: Maintains blood glucose levels through glycogen degradation and specific G6P phosphatase expression.

    • Other Tissues: Small glycogen stores for brief energy needs.

Page 2: Glycogen Structure

  • Glycogen is a polymer with one reducing end and numerous non-reducing ends.

  • Glucosyl residues linked by C1-C4 (α(1→4) linkages); branches at C1-C6 every 8-14 residues.

  • Importance of Branches:

    • Multiple synthesis and degradation sites.

    • Non-reducing ends: Where glucose is released during degradation.

Page 3: Glycogen Metabolism

  • Distinct pathways for synthesis and breakdown due to energy requirements.

  • Enzymes Involved in Breakdown:

    • Glycogen phosphorylase (Glycogen → G1P).

    • Phosphoglucomutase (G1P ⇌ G6P).

    • UDP-glucose pyrophosphorylase (G1P + UTP → UDP-glucose).

    • Glycogen synthase (UDP-glucose → Glycogen).

  • Rate Limiting Enzymes:

    • Glycogen phosphorylase and glycogen synthase.

Page 4: Synthesis of UDP-Glucose

  • UDP-glucose synthesis from G1P and UTP is thermodynamically unfavorable, energy input required.

  • Reaction: G1P + UTP catalyzed by UDP-glucose pyrophosphorylase.

  • Product: UDP-glucose, an activated donor of glucosyl units.

Page 5: Glycogen Chain Elongation

  • Glycogen synthase adds glucose units from UDP-glucose to glycogen’s non-reducing ends, forming α(1→4) bonds.

  • Energetics: Glycogen + G1P + UTP → Glycogen + UDP + 2Pi (energy cost).

  • UTP replenishment through nucleoside diphosphate kinase.

  • Regulation: Glycogen synthase is inhibited by ATP, ADP, and Pi; activated by G6P.

Page 6: Glycogenin Function

  • Glycogenin primes glycogen synthesis by adding glucose residues to itself, starting the glycogen chain.

  • Mechanism involves transferring glucose from UDPG and elongating the chain before glycogen synthase takes over.

  • Branching enzyme creates α(1→6) branches every 11 residues.

Page 7: Glycogen Breakdown Process

  • Steps include:

    1. Generation of G1P (Glycogen phosphorylase).

    2. Debranching (Debranching enzyme).

    3. Conversion of G1P to G6P (Phosphoglucomutase).

Page 8: G1P Generation

  • Glycogen phosphorylase catalyzes the phosphorolysis of glycogen into G1P.

  • Regulation includes allosteric interactions and covalent modifications (phosphorylation).

  • Allosteric control: High ATP inhibits, high AMP activates.

Page 9: Debranching Steps

  • Utilizes two enzyme activities:

    1. Transfers trisaccharides (α(1→4) glucosyltransferase).

    2. Hydrolyzes glycosidic bond (α(1→6) glucosidase).

  • Majority of glycogen converts to G1P, some to glucose.

Page 10: G6P Conversion

  • Phosphoglucomutase converts G1P to G6P for metabolic pathways.

  • The conversion process includes a phosphoryl transfer, and the reaction is reversible.

Page 11: Summary of Glycogen Metabolism

  • Muscle uses G6P for glycolysis; liver converts it to glucose for blood circulation.

  • Glycogen breakdown efficiency: consume 2 ATP for synthesis, generate 33 ATP during breakdown, totaling 97% efficiency.

Page 12: Enzyme Cascades

  • Covalent modification mechanisms: reversible (e.g., phosphorylation) and irreversible.

  • Monocyclic and bicyclic cascades modify enzymes E and F as signals for glycogen metabolism.

Page 13: Glycogen Phosphorylase Regulation

  • Two states: T (inactive) and R (active);

    • Allosteric activators/inhibitors affect activity based on physiological conditions.

Page 14: Phosphorylase Kinase Role

  • Activates glycogen phosphorylase and inactivates synthase through phosphorylation.

  • Its activity is regulated by calcium levels and hormonal signals.

Page 15: PKA Regulation

  • PKA activated by cAMP; influences glycogen breakdown and inhibits glycogen synthase.

Page 16: Glycogen Synthase Regulation

  • Phosphorylated form is inactive; dephosphorylation activates synthase, influenced by insulin signaling.

Page 17: PP1c Activity Regulation

  • PP1c facilitates glycogen synthesis by regulating glycogen synthase and phosphorylase activities.

Page 18: Hormonal Regulation

  • Insulin signaling inactivates glycogen synthase kinase, activating glycogen synthesis.

Page 19: Glycogen Synthesis Mechanism

  • Insulin activates pathways to increase glycogen synthase activity.

Page 20: Glycogen Breakdown Mechanism

  • Hormonal signals activate PKA, trigger glycogen breakdown via phosphorylase kinase.

Page 21: External Signaling Mechanism

  • Hormonal signaling pathways affect cellular responses and glycogen metabolism.

Page 22: Regulation of Muscle vs Liver

  • Both tissues respond to hormones, but differ in receptors and signaling pathways for glycogen metabolism.

Page 23: Muscle Glycogen Synthesis

  • Mechanisms involve high insulin and glucose levels, activating glycogen synthase.

Page 24: Liver Glycogen Synthesis

  • Insulin inhibits GSK3β, enabling synthesis and dephosphorylation of glycogen synthase.

Page 25: Liver Glycogen Breakdown

  • Stress hormones and glucagon trigger glycogen breakdown pathways in the liver.

Page 26: Glycogen Storage Diseases

  • Type 1 (G6P deficiency): Symptoms include liver enlargement and hypoglycemia.

    • Type 5 (Muscle phosphorylase deficiency): Leads to exercise cramps.

    • Type 6 (Liver phosphorylase deficiency): Causes hypoglycemia due to impaired glycogen breakdown.

Page 27: Pyruvate Dehydrogenase Complex (PDC)

  • Enzyme complex catalyzing pyruvate to Acetyl-CoA in mitochondria, crucial for aerobic metabolism.

Page 28: PDC Structure

  • Composed of multiple enzymes requiring various coenzymes (TPP, lipoic acid, CoA, FAD, NAD+).

Page 29: PDC Reactions

  • Overview of enzymatic functions and substrate channeling.

Page 30: E2 Functionality

  • Role of CoA substitution and generation of high-energy Acetyl-CoA.

Page 31: E3 Functionality

  • Restoration of E2 and own FAD for subsequent reactions; generates NADH.

Page 32: PDC Regulation

  • Controlled by product inhibition and phosphorylation/dephosphorylation of E1.

Page 33: Phosphorylation Effects

  • Inactivation through PDK and activation through PDP based on cellular energy state.

Page 34: Citric Acid Cycle (CAC)

  • Series of reactions generating CO2, NADH, and GTP/ATP; connects to metabolic pathways.

Page 35: Key Enzymes in CAC

  • Citrate synthase and aconitase notable for C-C bond formation and isomerization.

Page 36: Additional CAC Enzymes

  • Isocitrate and α-KG dehydrogenases facilitate NADH and GTP generation during oxidative decarboxylation.

Page 37: Succinyl-CoA Generation

  • Produces GTP/ATP and marks completion of one acetyl-CoA oxidation.

Page 38: CAC Recycling Steps

  • Include succinate dehydrogenase, fumarase, and malate dehydrogenase.

Page 39: Energy Balance Sheet

  • Comprehensive overview of ATP generation from glycolysis, PDC, and CAC.

Page 40: CAC Regulation

  • Three key enzymes regulated by substrate availability and product inhibition.

Page 41: Regulation of Isocitrate Dehydrogenase

  • Product inhibition by NADH and allosteric activation by ADP.

Page 42: α-Ketoglutarate Dehydrogenase Regulation

  • Inhibited by NADH and succinyl-CoA; activated by Ca2+.

Page 43: Summary of Regulatory Points

  • Highlight communication pathways in metabolic regulation.

Page 44: CAC Functions

  • Influences energy state, redox state, and availability of key compounds.

Page 45: Anaplerotic Reactions

  • Replenish CAC intermediates; include pyruvate carboxylase and transamination reactions.

Page 46: Overview of Key Transition Reactions

  • Key conversions and regulatory points in metabolism are summarized.

Page 47: Mitochondrial Structure

  • Description of mitochondrial components and their functions in oxidative phosphorylation.

Page 48: Electron Transport Chain (ETC)

  • Details of electron flow through mitochondrial complexes and their role in proton gradient generation.

Page 49: H+ Translocation Coupling

  • Mechanism of H+ flow and energy release as electrons pass through the ETC.

Page 50: Alternative CoQ Reduction Pathways

  • Various pathways contribute to the reduction of CoQ for electron transfer.

Page 51: The Q Cycle

  • Mechanism detailing electron transfer at Complex III for efficient energy production.

Page 52: Complex IV Functions

  • Key role in converting electrons from CytC into water, with proton pumping action.

Page 53: ATP Synthesis Mechanism

  • F1 sector of ATP synthase generates ATP through rotation; processes involved in catalysis.

Page 54: P/O Ratio

  • Explanation of ATP production efficiency in relation to oxygen consumption.

Page 55: Evidence of Chemiosmotic Coupling

  • Various observations support the chemiosmotic theory of ATP synthesis.

Page 56: Mitochondrial Chemical Uncouplers

  • Functional impacts of uncouplers on respiration and ATP synthesis.

Page 57: Mitochondrial Origins

  • Historical evolution, including endosymbiotic events leading to modern organelles.

Page 58: Mitochondrial DNA

  • Distinctive traits, genes present, and reliance on nuclear genes for mitochondrial function.

Page 59: Mitochondrial Diseases

  • Impact of mtDNA mutations and nucleotide coordination on cellular health and metabolism.

Page 60: Respiratory Control Mechanisms

  • ATP utilization and its effect on electron flow and oxygen consumption rates.