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Control of Glycolysis and Glycogen Metabolism

Richard J. Connett, Kent Sahlin

10.1002/cphy.cp120119

Source: Supplement 29: Handbook of Physiology, Exercise: Regulation and Integration of Multiple Systems

Originally published: 1996

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Importance of Glycolysis in Skeletal Muscle at Rest and During Exercise
2 General Overview of the Glycolytic Pathway
2.1 ATP Supply
2.2 Support of Other Metabolic Needs
3 Properties of Glycogen and Associated Enzymes
3.1 Structure of Glycogen
3.2 Control of GP
3.3 Control of GS
3.4 Integrated Control of GP and GS During Exercise
4 Other Specific Glycolytic Enzyme Controls
4.1 Equilibrium Group
4.2 Phosphofructokinase
4.3 Aldolase
4.4 Glyceraldehydephosphate Dehydrogenase and Phosphoglycerate Kinase (PGK)
4.5 Phosphoglycerate Mutase and Enolase
4.6 Pyruvate Kinase
4.7 Lactate Dehydrogenase
5 Carbohydrate Utilization at Rest and During Exercise
5.1 Diurnal Variations of Body Stores at Rest
5.2 CHO Utilization during Exercise
5.3 Control of Glycogenolysis during Heavy Exercise
6 Postexercise Glycogen Synthesis and its Control
6.1 Resynthesis of Muscle Glycogen After Exercise
6.2 Regulatory Mechanisms
7 Muscle Glycogen Metabolism and Fatigue
7.1 Importance of CHO during Prolonged Exercise
7.2 Importance of Glycogen during High‐Intensity Exercise
8 Integrative Aspects of Glycolytic Control and Future Directions (K. Sahlin)
8.1 Rest‐Work Transition
8.2 Future Directions
9 Integrative Aspects of Glycolytic Control and Future Directions (R. J. Connett)
9.1 Systems Analysis
9.2 Cellular Oxygen Tension and Lactate Formation
9.3 Summary
9.4 State of the Phosphate Energy System
9.5 Cytosolic pH
9.6 Substrate Effects
9.7 Future Directions
Figure 1. Figure 1.

Schematic diagram of biochemical system in muscle. Subsystems are indicated by rectangles. Those with a T indicate specialized transport systems. Important reactant pools are shown in ellipses. Solid arrows indicate material flow; dashed arrows, flow of information.
Figure 2. Figure 2.

Metabolic pathways of glycogen metabolism. Numbers refer to the following enzymes: 1, glycogen phosphorylase; 2, UDP‐glucose pyrophosphorylase; 3, glycogen synthase; 4, branching enzyme; 5, debranching enzyme; 6, hexokinase; 7, phosphog‐lucomutase; 8, phosphoglucose isomerase.
Figure 3. Figure 3.

Control of glycogenolysis by phosphorylation/dephos‐phorylation of glycogen phosphorylase. cAMP‐PK, cAMP‐dependent protein kinase; Epi, epinephrine; Ins‐PK, insulin‐dependent protein kinase; PKb, unphosphorylated protein kinase; PKa, phosphorylated protein kinase; PP, protein phosphatase; GPa, glycogen phosphorylase a; GPb, glycogen phosphorylase b. Filled arrows denote enzymatic reaction or connect active enzyme with catalyzed reaction. Dashed arrows connect enzyme, which can be active under some conditions with catalyzed reaction. Dotted arrows denote activation (+) or inhibition (‐) of indicated enzyme. All substrates and products in metabolic reactions are not shown.
Figure 4. Figure 4.

Control of glycogen synthesis by covalent modification of glycogen synthase. GSd, phosphorylated glycogen synthase (G6P dependent form); GSi, unphosphorylated glycogen synthase; PK, Ca2+‐dependent and other protein kinases; G6P, glucose 6‐phosphate. See legend of Figure 3 for further details.
Figure 5. Figure 5.

Control of glycogenolysis during exercise. The feedback inhibition of GP by increases in H+ may involve both reduced covalent activation of GP, decreased availability of active substrate (), and allosteric inhibition of Gpb by increases in G6P occurring secondary to inhibition of PFK. See text for further details. cAMP‐Pk, cAMP‐dependent protein kinase; Epi, epinephrine; Ins‐Pk, insulin‐dependent protein kinase; PP, protein phosphatase; GPa, glycogen phosphorylase a; GPb, glycogen phosphorylase b; Pkb, unphosphorylated protein kinase; Pka, phosphorylated protein kinase; Gsd, phosphorylated glycogen synthase; GSi, unphosphorylated gycogen synthase; Pk, Ca2+‐dependent and other protein kinase si GGP, glucose G‐phosphate.
Figure 6. Figure 6.

Outline of the glycolytic pathway from G6P to lactate. Solid lines show reactions. Dashed line indicates pathways included in Figure 2. G6P, glucose 6‐phosphate; F6P, fructose 6‐phosphate; FDP, fructose 1,6‐bisphosphate; DHAP, dihydrox‐yacetone phosphate; GA3P, glyceraldehyde 3‐phosphate; 3PG, 3‐phosphoglycerate; 2PG, 2‐phosphoglycerate; PEP, phosphoenolpyruvate. Numbers refer to enzymes: 1, hexokinase; 2, phosphoglucoisomerase; 3, phosphofructokinase (PFK); 4, aldolase; 5, triosephosphate isomerase; 6, combined glyceraldehyde phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK) steps; 7, phosphoglycerate mutase; 8, enolase; 9, pyruvate kinase; 10, lactate dehydrogenase (LDH).
Figure 7. Figure 7.

Rate of pyruvate formation and pyruvate oxidation in muscle at rest and during exercise in muscle at different workloads. Rate of pyruvate oxidation was calculated from O2 consumption and estimated or measured respiratory exchange ratio. Rate of pyruvate production was calculated from the accumulation in muscle of lactate, pyruvate, alanine, and acetylcarnitine + release of lactate + rate of pyruvate oxidation. (Data are from 147, 232, 233.)
Figure 8. Figure 8.

Normalized metabolite concentrations as a function of high‐energy phosphate. All values were computed using pH = 7.0, [Mg2+] = 1 mM, and total free adenine nucleotide pool (ADt) = 0.2 × total creatine pool. Fc, [PCr]/[total creatine]; Ratp, [ATP]/[ADt]; Radp, [ADP]/[ADt]; Ramp, [AMP]/[ADt]; Fpe, ([PCr] + 2[ATP] + ADP])/[total creatine].

After Connett 52
Figure 9. Figure 9.

Schematic of cytosolic redox subsystem. GAPDH, glyceraldehydephosphate dehydrogenase; GPDH, glycerolphosphate dehydrogenase; LDH, lactate dehydrogenase.
Figure 10. Figure 10.

Relationship between cytosolic redox potential and . Correlation between cytosolic redox potential as estimated from the [lactate]/[pyruvate] ratio and oxygen consumption in dog gracilis muscle.

From Connett and Gayeski 59
Figure 11. Figure 11.

System controls on glycolysis. Solid lines show carbon flow in pathway. Other lines indicate control interactions either allosteric or substrate effects. Details are given in the text.


Figure 1.

Schematic diagram of biochemical system in muscle. Subsystems are indicated by rectangles. Those with a T indicate specialized transport systems. Important reactant pools are shown in ellipses. Solid arrows indicate material flow; dashed arrows, flow of information.



Figure 2.

Metabolic pathways of glycogen metabolism. Numbers refer to the following enzymes: 1, glycogen phosphorylase; 2, UDP‐glucose pyrophosphorylase; 3, glycogen synthase; 4, branching enzyme; 5, debranching enzyme; 6, hexokinase; 7, phosphog‐lucomutase; 8, phosphoglucose isomerase.



Figure 3.

Control of glycogenolysis by phosphorylation/dephos‐phorylation of glycogen phosphorylase. cAMP‐PK, cAMP‐dependent protein kinase; Epi, epinephrine; Ins‐PK, insulin‐dependent protein kinase; PKb, unphosphorylated protein kinase; PKa, phosphorylated protein kinase; PP, protein phosphatase; GPa, glycogen phosphorylase a; GPb, glycogen phosphorylase b. Filled arrows denote enzymatic reaction or connect active enzyme with catalyzed reaction. Dashed arrows connect enzyme, which can be active under some conditions with catalyzed reaction. Dotted arrows denote activation (+) or inhibition (‐) of indicated enzyme. All substrates and products in metabolic reactions are not shown.



Figure 4.

Control of glycogen synthesis by covalent modification of glycogen synthase. GSd, phosphorylated glycogen synthase (G6P dependent form); GSi, unphosphorylated glycogen synthase; PK, Ca2+‐dependent and other protein kinases; G6P, glucose 6‐phosphate. See legend of Figure 3 for further details.



Figure 5.

Control of glycogenolysis during exercise. The feedback inhibition of GP by increases in H+ may involve both reduced covalent activation of GP, decreased availability of active substrate (), and allosteric inhibition of Gpb by increases in G6P occurring secondary to inhibition of PFK. See text for further details. cAMP‐Pk, cAMP‐dependent protein kinase; Epi, epinephrine; Ins‐Pk, insulin‐dependent protein kinase; PP, protein phosphatase; GPa, glycogen phosphorylase a; GPb, glycogen phosphorylase b; Pkb, unphosphorylated protein kinase; Pka, phosphorylated protein kinase; Gsd, phosphorylated glycogen synthase; GSi, unphosphorylated gycogen synthase; Pk, Ca2+‐dependent and other protein kinase si GGP, glucose G‐phosphate.



Figure 6.

Outline of the glycolytic pathway from G6P to lactate. Solid lines show reactions. Dashed line indicates pathways included in Figure 2. G6P, glucose 6‐phosphate; F6P, fructose 6‐phosphate; FDP, fructose 1,6‐bisphosphate; DHAP, dihydrox‐yacetone phosphate; GA3P, glyceraldehyde 3‐phosphate; 3PG, 3‐phosphoglycerate; 2PG, 2‐phosphoglycerate; PEP, phosphoenolpyruvate. Numbers refer to enzymes: 1, hexokinase; 2, phosphoglucoisomerase; 3, phosphofructokinase (PFK); 4, aldolase; 5, triosephosphate isomerase; 6, combined glyceraldehyde phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK) steps; 7, phosphoglycerate mutase; 8, enolase; 9, pyruvate kinase; 10, lactate dehydrogenase (LDH).



Figure 7.

Rate of pyruvate formation and pyruvate oxidation in muscle at rest and during exercise in muscle at different workloads. Rate of pyruvate oxidation was calculated from O2 consumption and estimated or measured respiratory exchange ratio. Rate of pyruvate production was calculated from the accumulation in muscle of lactate, pyruvate, alanine, and acetylcarnitine + release of lactate + rate of pyruvate oxidation. (Data are from 147, 232, 233.)



Figure 8.

Normalized metabolite concentrations as a function of high‐energy phosphate. All values were computed using pH = 7.0, [Mg2+] = 1 mM, and total free adenine nucleotide pool (ADt) = 0.2 × total creatine pool. Fc, [PCr]/[total creatine]; Ratp, [ATP]/[ADt]; Radp, [ADP]/[ADt]; Ramp, [AMP]/[ADt]; Fpe, ([PCr] + 2[ATP] + ADP])/[total creatine].

After Connett 52


Figure 9.

Schematic of cytosolic redox subsystem. GAPDH, glyceraldehydephosphate dehydrogenase; GPDH, glycerolphosphate dehydrogenase; LDH, lactate dehydrogenase.



Figure 10.

Relationship between cytosolic redox potential and . Correlation between cytosolic redox potential as estimated from the [lactate]/[pyruvate] ratio and oxygen consumption in dog gracilis muscle.

From Connett and Gayeski 59


Figure 11.

System controls on glycolysis. Solid lines show carbon flow in pathway. Other lines indicate control interactions either allosteric or substrate effects. Details are given in the text.

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Article Title: Control of Glycolysis and Glycogen Metabolism
 

How to Cite

Richard J. Connett, Kent Sahlin. Control of Glycolysis and Glycogen Metabolism. Compr Physiol 2011, Supplement 29: Handbook of Physiology, Exercise: Regulation and Integration of Multiple Systems: 870-911. First published in print 1996. doi: 10.1002/cphy.cp120119