{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T05:28:17Z","timestamp":1786426097044,"version":"build-2736575974"},"reference-count":106,"publisher":"MDPI AG","issue":"16","license":[{"start":{"date-parts":[[2026,8,8]],"date-time":"2026-08-08T00:00:00Z","timestamp":1786147200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int. J. Mol. Sci.","IJMS"],"abstract":"<jats:p>Glycogenolysis is an important contributor to ATP production in contracting skeletal muscle. However, the activation of glycogen phosphorylase in resting muscle does not by itself trigger significant glycogenolysis. To elucidate the mechanisms underlying this regulation, we analyzed the functional coupling between glycogenolysis and glycolysis using a mathematical model of energy metabolism in mammalian fast-twitch (white) skeletal muscle. A system-level analysis of the model reveals an important role for inorganic phosphate (a substrate for glycogen phosphorylase) in regulating glycogenolysis rates in both resting and contracting muscle. In contracting muscle, at sufficiently high concentrations of inorganic phosphate, the activation of glycogen phosphorylase markedly increases the rate of glycogenolysis, thereby enhancing ATP production and stabilizing the cellular energy charge. In contrast, glycogen phosphorylase activation in resting muscle is unable to support glycogen breakdown due to a significant decrease in inorganic phosphate levels. Moreover, the analysis shows that forced acceleration of the glycogen phosphorylase reaction under resting conditions does not increase ATP production; instead, it promotes the accumulation of phosphorylated glycolytic intermediates, which may induce osmotic stress and cause damage to muscle cells.<\/jats:p>","DOI":"10.3390\/ijms27167106","type":"journal-article","created":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T09:24:53Z","timestamp":1786353893000},"page":"7106","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Activation of ATP Consumption Is Necessary to Stimulate Glycogenolysis in Skeletal Muscle"],"prefix":"10.3390","volume":"27","author":[{"given":"Michael V.","family":"Martinov","sequence":"first","affiliation":[{"name":"Center for Theoretical Problems of Physico-Chemical Pharmacology, Russian Academy of Sciences, Moscow 109029, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetlana I.","family":"Sudarkina","sequence":"additional","affiliation":[{"name":"Faculty of Computer Sciences, National Research University Highest School of Economics, Moscow 109028, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fazoil I.","family":"Ataullakhanov","sequence":"additional","affiliation":[{"name":"Center for Theoretical Problems of Physico-Chemical Pharmacology, Russian Academy of Sciences, Moscow 109029, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6251-6115","authenticated-orcid":false,"given":"Victor M.","family":"Vitvitsky","sequence":"additional","affiliation":[{"name":"Center for Theoretical Problems of Physico-Chemical Pharmacology, Russian Academy of Sciences, Moscow 109029, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"K\u00f6nig, M., Bulik, S., and Holzh\u00fctter, H.-G. (2012). Quantifying the Contribution of the Liver to Glucose Homeostasis: A Detailed Kinetic Model of Human Hepatic Glucose Metabolism. PLoS Comput. Biol., 8.","DOI":"10.1371\/journal.pcbi.1002577"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"E11","DOI":"10.1152\/ajpendo.90563.2008","article-title":"Four Grams of Glucose","volume":"296","author":"Wasserman","year":"2009","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.bbacli.2016.02.001","article-title":"Glycogen Metabolism in Humans","volume":"5","year":"2016","journal-title":"BBA Clin."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1007\/s00421-022-04935-1","article-title":"A Century of Exercise Physiology: Key Concepts in Regulation of Glycogen Metabolism in Skeletal Muscle","volume":"122","author":"Katz","year":"2022","journal-title":"Eur. J. Appl. Physiol."},{"key":"ref_5","unstructured":"Rowell, L.B., and Shepherd, J.T. (1996). Control of Glycolysis and Glycogen Metabolism. Handbook of Phisiology, Oxphord University Press."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"E958","DOI":"10.1152\/ajpendo.00190.2003","article-title":"Hexokinase II Partial Knockout Impairs Exercise-Stimulated Glucose Uptake in Oxidative Muscles of Mice","volume":"285","author":"Fueger","year":"2003","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1038\/s42255-020-0251-4","article-title":"Skeletal Muscle Energy Metabolism during Exercise","volume":"2","author":"Hargreaves","year":"2020","journal-title":"Nat. Metab."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/0003-9861(61)90118-7","article-title":"The Metabolism of the Tonic and Tetanic Muscles I. Glycolytic Metabolism","volume":"95","author":"Domonkos","year":"1961","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1113\/jphysiol.1994.sp020238","article-title":"The Metabolic Responses of Human Type I and II Muscle Fibres during Maximal Treadmill Sprinting","volume":"478","author":"Greenhaff","year":"1994","journal-title":"J. Physiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3301","DOI":"10.1016\/S0021-9258(18)95910-7","article-title":"Allosteric Properties of Phosphorylase b. II. Comparison with a Kinetic Model","volume":"242","author":"Madsen","year":"1967","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0301-4622(01)00189-2","article-title":"Combined Kinetic Mechanism Describing Activation and Inhibition of Muscle Glycogen Phosphorylase b by Adenosine 5\u2032-Monophosphate","volume":"92","author":"Klinov","year":"2001","journal-title":"Biophys. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2071","DOI":"10.1152\/jappl.2001.91.5.2071","article-title":"Skeletal Muscle Glycogen Phosphorylase a Kinetics: Effects of Adenine Nucleotides and Caffeine","volume":"91","author":"Rush","year":"2001","journal-title":"J. Appl. Physiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"11957","DOI":"10.1021\/bi7005527","article-title":"Enzyme Kinetics of Muscle Glycogen Phosphorylase b","volume":"46","author":"Walcott","year":"2007","journal-title":"Biochemistry"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2564","DOI":"10.1016\/S0021-9258(18)63108-4","article-title":"Kinetic Mechanism of Rabbit Muscle Glycogen Phosphorylase a","volume":"245","author":"Gold","year":"1970","journal-title":"J. Biol. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2440","DOI":"10.1016\/S0021-9258(18)93872-X","article-title":"Regulatipon of Glycogenolysis in Muscle. 3. Mucle Glycogen Phosphorylase Activity","volume":"239","author":"Morgan","year":"1964","journal-title":"J. Biol. Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1042\/bj3280083","article-title":"Kinetic Mechanism of the Glycogen-Phosphorylase-Catalysed Reaction in the Direction of Glycogen Synthesis: Co-Operative Interactions of AMP and Glucose 1-Phosphate during Catalysis","volume":"328","author":"Sergienko","year":"1997","journal-title":"Biochem. J."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/296613a0","article-title":"The Role of Protein Phosphorylation in Neural and Hormonal Control of Cellular Activity","volume":"296","author":"Cohen","year":"1982","journal-title":"Nature"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1007\/s00335-014-9519-x","article-title":"Regulation of Glycogen Breakdown and Its Consequences for Skeletal Muscle Function after Training","volume":"25","author":"Katz","year":"2014","journal-title":"Mamm. Genome"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2243","DOI":"10.1152\/jappl.1989.67.6.2243","article-title":"Regulation of Glycogenolysis in Human Skeletal Muscle","volume":"67","author":"Ren","year":"1989","journal-title":"J. Appl. Physiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1152\/jappl.1982.53.3.708","article-title":"Regulation of Glycogenolysis in Human Muscle at Rest and during Exercise","volume":"53","author":"Chasiotis","year":"1982","journal-title":"J. Appl. Physiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"E890","DOI":"10.1152\/ajpendo.1999.277.5.E890","article-title":"Regulation of Skeletal Muscle Glycogen Phosphorylase and PDH during Maximal Intermittent Exercise","volume":"277","author":"Parolin","year":"1999","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1152\/jappl.1990.69.3.919","article-title":"Regulation of Phosphorylase a Activity in Human Skeletal Muscle","volume":"69","author":"Ren","year":"1990","journal-title":"J. Appl. Physiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1097\/00005768-200004000-00007","article-title":"An Enzymatic Approach to Lactate Production in Human Skeletal Muscle during Exercise","volume":"32","author":"Spriet","year":"2000","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"C409","DOI":"10.1152\/ajpcell.1990.259.3.C409","article-title":"Influence of ATP Turnover and Metabolite Changes on IMP Formation and Glycolysis in Rat Skeletal Muscle","volume":"259","author":"Sahlin","year":"1990","journal-title":"Am. J. Physiol.-Cell Physiol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1152\/jappl.1983.54.1.45","article-title":"Regulation of Glycogenolysis in Human Muscle in Response to Epinephrine Infusion","volume":"54","author":"Chasiotis","year":"1983","journal-title":"J. Appl. Physiol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/0010-4809(68)90009-8","article-title":"Simulation of the Detailed Regulation of Glycolysis in a Heart Supernatant Preparation","volume":"2","author":"Garfinkel","year":"1968","journal-title":"Comput. Biomed. Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1006\/abbi.1998.0643","article-title":"Control Analysis of Muscle Glycogen Metabolism","volume":"353","author":"Schulz","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1114\/1.1492813","article-title":"A Computational Model for Glycogenolysis in Skeletal Muscle","volume":"30","author":"Lambeth","year":"2002","journal-title":"Ann. Biomed. Eng."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1113\/expphysiol.2009.049841","article-title":"Silencing of Glycolysis in Muscle: Experimental Observation and Numerical Analysis","volume":"95","author":"Schmitz","year":"2010","journal-title":"Exp. Physiol."},{"key":"ref_30","unstructured":"Palm, D.C. (2013). The Regulatory Design of Glycogen Metabolism in Mammalianskeletal Muscle. [Ph.D. Thesis, University of Stellenbosch]."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"C25","DOI":"10.1152\/ajpcell.00094.2008","article-title":"Role of NADH\/NAD+ Transport Activity and Glycogen Store on Skeletal Muscle Energy Metabolism during Exercise: In Silico Studies","volume":"296","author":"Li","year":"2009","journal-title":"Am. J. Physiol.-Cell Physiol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"129687","DOI":"10.1016\/j.bbagen.2020.129687","article-title":"Kinetic Modeling of Glucose Central Metabolism in Hepatocytes and Hepatoma Cells","volume":"1864","author":"Saavedra","year":"2020","journal-title":"Biochim. Biophys. Acta BBA-Gen. Subj."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1111\/j.1432-1033.1981.tb05246.x","article-title":"The Regulation of Glycolysis in Human Erythrocytes: The Dependence of the Glycolytic Flux on the ATP Concentration","volume":"115","author":"Ataullakhanov","year":"1981","journal-title":"Eur. J. Biochem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1023\/A:1022069718709","article-title":"What Determines the Intracellular ATP Concentration","volume":"22","author":"Ataullakhanov","year":"2002","journal-title":"Biosci. Rep."},{"key":"ref_35","first-page":"76","article-title":"Principles of Regulation of Stationary Functioning Metabolic Systems","volume":"53","author":"Ataullakhanov","year":"2022","journal-title":"Uspekhi Phisiologicheskih Nauk"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Martinov, M.V., Ataullakhanov, F.I., and Vitvitsky, V.M. (2026). The Critical Role of Adenylate Kinase in Regulating the Glycolysis Rate in Cells. Int. J. Mol. Sci., 27.","DOI":"10.3390\/ijms27052479"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1152\/jappl.1986.61.1.54","article-title":"Human Muscle Metabolism during Sprint Running","volume":"61","author":"Cheetham","year":"1986","journal-title":"J. Appl. Physiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/j.1748-1716.1988.tb08386.x","article-title":"Skeletal Muscle Glucolysis, Glycogenolysis and Glycogen Phosphorylase during Electrical Stimulation in Man","volume":"133","author":"Ren","year":"1988","journal-title":"Acta Physiol. Scand."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"E132","DOI":"10.1152\/ajpendo.1998.275.1.E132","article-title":"Effects of Short-Term Submaximal Training in Humans on Muscle Metabolism in Exercise","volume":"275","author":"Putman","year":"1998","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1203\/00006450-197603000-00001","article-title":"Control of Glycolysis in Skeletal Muscle from Fetal Rhesus Monkeys","volume":"10","author":"Beatty","year":"1976","journal-title":"Pediatr. Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/0885-4505(86)90081-2","article-title":"Regulation of Muscle Pyruvate Metabolism during Exercise","volume":"35","author":"Dohm","year":"1986","journal-title":"Biochem. Med. Metab. Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"109","DOI":"10.3109\/00365517409082477","article-title":"Glycogen, Glycolytic Intermediates and High-Energy Phosphates Determined in Biopsy Samples of Musculus Quadriceps Femoris of Man at Rest. Methods and Variance of Values","volume":"33","author":"Harris","year":"1974","journal-title":"Scand. J. Clin. Lab. Investig."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Irimia, J.M., Rovira, J., Nielsen, J.N., Guerrero, M., Wojtaszewski, J.F.P., and Cuss\u00f3, R. (2012). Hexokinase 2, Glycogen Synthase and Phosphorylase Play a Key Role in Muscle Glycogen Supercompensation. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0042453"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"374","DOI":"10.2337\/diab.17.6.374","article-title":"Effects of Plasma Albumin on Glycolytic Intermediates in Rat Diaphragm Muscle","volume":"17","author":"Karl","year":"1968","journal-title":"Diabetes"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"E380","DOI":"10.1152\/ajpendo.1993.265.3.E380","article-title":"Regulation of Endogenous Fat and Carbohydrate Metabolism in Relation to Exercise Intensity and Duration","volume":"265","author":"Romijn","year":"1993","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1152\/physrev.00038.2012","article-title":"Exercise, GLUT4, and Skeletal Muscle Glucose Uptake","volume":"93","author":"Richter","year":"2013","journal-title":"Physiol. Rev."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1152\/jappl.1993.75.2.712","article-title":"Human Muscle Metabolism during Intermittent Maximal Exercise","volume":"75","author":"Gaitanos","year":"1993","journal-title":"J. Appl. Physiol."},{"key":"ref_48","first-page":"483","article-title":"Quantitative model of human erythrocyte glycolysis. I. Relationship between the stationary rate of glycolysis and the ATP concentration","volume":"22","author":"Ataullakhanov","year":"1977","journal-title":"Biofizika"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/0300-9084(89)90071-0","article-title":"Control, Regulation and Thermodynamics of Free-Energy Transduction","volume":"71","author":"Westerhoff","year":"1989","journal-title":"Biochimie"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Cornish-Bowden, A., and C\u00e1rdenas, M.L. (1990). Control of Metabolic Processes, Springer.","DOI":"10.1007\/978-1-4757-9856-2"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Heinrich, R., and Schuster, S. (1996). The Regulation of Cellular Systems, Chapman & Hall [u.a.].","DOI":"10.1007\/978-1-4613-1161-4"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"E65","DOI":"10.1152\/ajpendo.1986.251.1.E65","article-title":"Leg Glucose Uptake during Maximal Dynamic Exercise in Humans","volume":"251","author":"Katz","year":"1986","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1042\/bj2450551","article-title":"Redox State and Lactate Accumulation in Human Skeletal Muscle during Dynamic Exercise","volume":"245","author":"Sahlin","year":"1987","journal-title":"Biochem. J."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"905612","DOI":"10.1155\/2010\/905612","article-title":"Interaction among Skeletal Muscle Metabolic Energy Systems during Intense Exercise","volume":"2010","author":"Baker","year":"2010","journal-title":"J. Nutr. Metab."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1007\/BF00585514","article-title":"Effects of Different Patterns of Long-Term Stimulation on Blood Flow, Fuel Uptake and Enzyme Activities in Rabbit Fast Skeletal Muscles","volume":"402","author":"Hudlicka","year":"1984","journal-title":"Pfl\u00fcg. Arch. Eur. J. Physiol."},{"key":"ref_56","unstructured":"Newsholme, E.A., and Start, C. (1973). Regulation in Metabolism, John Wiley & Sons."},{"key":"ref_57","unstructured":"Rodwell, V., Bender, D., Botham, K., Kennely, P., and Weil, A. (2018). Harper\u2019s Illustrated Biochemistry, McGraw-Hill Education. [31st ed.]."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1111\/j.1748-1716.1985.tb07560.x","article-title":"The Effect of Adrenalin Infusion on the Regulation of Glycogenolysis in Human Muscle during Isometric Contraction","volume":"123","author":"Chasiotis","year":"1985","journal-title":"Acta Physiol. Scand."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1007\/s00424-019-02304-0","article-title":"Isoproterenol Enhances Force Production in Mouse Glycolytic and Oxidative Muscle via Separate Mechanisms","volume":"471","author":"Blackwood","year":"2019","journal-title":"Pfl\u00fcg. Arch.-Eur. J. Physiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1249\/00005768-199408000-00009","article-title":"Turnover of Human Muscle Glycogen with Low-Intensity Exercise","volume":"26","author":"Price","year":"1994","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1113\/jphysiol.2003.051078","article-title":"Contraction-mediated Glycogenolysis in Mouse Skeletal Muscle Lacking Creatine Kinase: The Role of Phosphorylase b Activation","volume":"553","author":"Katz","year":"2003","journal-title":"J. Physiol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"E791","DOI":"10.1152\/ajpendo.1992.262.6.E791","article-title":"Increased Plasma FFA Uptake and Oxidation during Prolonged Exercise in Trained vs. Untrained Humans","volume":"262","author":"Turcotte","year":"1992","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1113\/jphysiol.2002.028084","article-title":"Dissociation between Muscle Tricarboxylic Acid Cycle Pool Size and Aerobic Energy Provision during Prolonged Exercise in Humans","volume":"545","author":"Gibala","year":"2002","journal-title":"J. Physiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1056\/NEJM199001253220403","article-title":"Quantitation of Muscle Glycogen Synthesis in Normal Subjects and Subjects with Non-Insulin-Dependent Diabetes by13C Nuclear Magnetic Resonance Spectroscopy","volume":"322","author":"Shulman","year":"1990","journal-title":"N. Engl. J. Med."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"E761","DOI":"10.1152\/ajpendo.1993.265.5.E761","article-title":"Quantitation of Glycolysis and Skeletal Muscle Glycogen Synthesis in Humans","volume":"265","author":"Rossetti","year":"1993","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/bj1520173","article-title":"Creatine Kinase Equilibrium and Lactate Content Compared with Muscle pH in Tissue Samples Obtained after Isometric Exercise","volume":"152","author":"Sahlin","year":"1975","journal-title":"Biochem. J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"R291","DOI":"10.1152\/ajpregu.1979.237.5.R291","article-title":"Reversal of Phosphorylase Activation in Muscle despite Continued Contractile Activity","volume":"237","author":"Conlee","year":"1979","journal-title":"Am. J. Physiol.-Regul. Integr. Comp. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1042\/cs0720475","article-title":"AMP Deaminase Deficiency: Study of the Human Skeletal Muscle Purine Metabolism during Ischaemic Isometric Exercise","volume":"72","author":"Sinkeler","year":"1987","journal-title":"Clin. Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.3390\/ijms10041729","article-title":"Adenylate Kinase and AMP Signaling Networks: Metabolic Monitoring, Signal Communication and Body Energy Sensing","volume":"10","author":"Dzeja","year":"2009","journal-title":"Int. J. Mol. Sci."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3069","DOI":"10.1038\/s41598-020-59430-4","article-title":"Slc20a1\/Pit1 and Slc20a2\/Pit2 Are Essential for Normal Skeletal Myofiber Function and Survival","volume":"10","author":"Chande","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"C73","DOI":"10.1152\/ajpcell.00510.2003","article-title":"Phosphate Uptake and PiT-1 Protein Expression in Rat Skeletal Muscle","volume":"287","author":"Abraham","year":"2004","journal-title":"Am. J. Physiol.-Cell Physiol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1139\/o70-117","article-title":"Kinetic Mechanism of Phosphorylase a. I. Initial Velocity Studies","volume":"48","author":"Engers","year":"1970","journal-title":"Can. J. Biochem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/S0021-9258(18)73136-0","article-title":"The Kinetics of the Enzymatic Synthesis of Glycogen from Glucose-1-Phosphate","volume":"135","author":"Cori","year":"1940","journal-title":"J. Biol. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0304-4165(99)00218-4","article-title":"Deficiencies of Glycolytic Enzymes as a Possible Cause of Hemolytic Anemia","volume":"1474","author":"Martinov","year":"2000","journal-title":"Biochim. Biophys. Acta BBA-Gen. Subj."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1111\/j.1432-1033.1974.tb03429.x","article-title":"Kinetic Properties of the Phosphofructokinase from Erythrocytes of Rats and Rabbits: 1. The Influence of Potassium and Ammonium Ions and of Inorganic Phosphate","volume":"43","author":"Jacobasch","year":"1974","journal-title":"Eur. J. Biochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"6522","DOI":"10.1016\/S0021-9258(18)50399-9","article-title":"Effects of Free Magnesium Concentration and Ionic Strength on Equilibrium Constants for the Glyceraldehyde Phosphate Dehydrogenaseconstants and Phosphoglycerate Kinase Reactions","volume":"254","author":"Cornell","year":"1979","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1063\/1.555948","article-title":"Thermodynamics of Enzyme-Catalyzed Reactions: Part 2. Transferases","volume":"23","author":"Goldberg","year":"1994","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1145\/3539801","article-title":"Enabling New Flexibility in the SUNDIALS Suite of Nonlinear and Differential\/Algebraic Equation Solvers","volume":"48","author":"Gardner","year":"2022","journal-title":"ACM Trans. Math. Softw."},{"key":"ref_79","unstructured":"Doedel, E.J., Paffenroth, R.C., Champneys, F.R., Fairgrieve, T.F., Kuznetsov, Y.A., Sandstede, B., and Wang, X. (2001). AUTO 2000: Continuation and Bifurcation Software for Ordinary Differential Equations (with HomCont). Techol. Rep. Calif. Inst. Technol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/0006-291X(68)90638-4","article-title":"On the Activities of Some Enzymes Concerned with Glycolysis and Glycogenolysis in Extracts of Rabbit Skeletal Muscles","volume":"31","author":"Burleigh","year":"1968","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1212\/WNL.33.8.1049","article-title":"Muscle Phosphogylcerate Mutase (PGAM) Deficiency: A Second Case","volume":"33","author":"Bresolin","year":"1983","journal-title":"Neurology"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1042\/bj1980621","article-title":"Maximum Activities and Properties of Glucose 6-Phosphatase in Muscles from Vertebrates and Invertebrates","volume":"198","author":"Surholt","year":"1981","journal-title":"Biochem. J."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1111\/j.1432-1033.1969.tb00674.x","article-title":"Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic Organization","volume":"10","author":"Bass","year":"1969","journal-title":"Eur. J. Biochem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1042\/bj1130157","article-title":"The Activities of Some Enzymes Concerned with Energy Metabolism in Mammalian Muscles of Differing Pigmentation","volume":"113","author":"Burleigh","year":"1969","journal-title":"Biochem. J."},{"key":"ref_85","first-page":"722","article-title":"Enzyme Patterns in Human Tissues. II. Glycolytic Enzyme Patterns in Nonmalignant Human Tissues","volume":"24","author":"Shonk","year":"1964","journal-title":"Cancer Res."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"E567","DOI":"10.1152\/ajpendo.1989.257.4.E567","article-title":"Human Variation in Skeletal Muscle Fiber-Type Proportion and Enzyme Activities","volume":"257","author":"Simoneau","year":"1989","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1055\/s-2007-1024847","article-title":"Effects of Chronic Hypoxia on Muscle Enzyme Activities","volume":"11","author":"Howald","year":"1990","journal-title":"Int. J. Sports Med."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1113\/jphysiol.1986.sp016316","article-title":"Maximum Activities of Key Glycolytic and Oxidative Enzymes in Human Muscle from Differently Trained Individuals","volume":"381","author":"Blomstrand","year":"1986","journal-title":"J. Physiol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1152\/ajplegacy.1973.225.4.962","article-title":"Glycolytic Enzymes in Different Types of Skeletal Muscle: Adaptation to Exercise","volume":"225","author":"Baldwin","year":"1973","journal-title":"Am. J. Physiol.-Leg. Content"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1002\/ana.410130104","article-title":"Phosphoglycerate Kinase Deficiency: Another Cause of Recurrent Myoglobinuria","volume":"13","author":"DiMauro","year":"1983","journal-title":"Ann. Neurol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"B160","DOI":"10.1093\/gerona\/55.3.B160","article-title":"Glyceraldehyde-3-Phosphate Dehydrogenase Varies With Age in Glycolytic Muscles of Rats","volume":"55","author":"Lowe","year":"2000","journal-title":"J. Gerontol. A. Biol. Sci. Med. Sci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/0065-2571(75)90025-4","article-title":"Some Aspects of Regulation of Enzyme Levels in Muscle Energy-Supplying Metabolism","volume":"13","author":"Pette","year":"1975","journal-title":"Adv. Enzym. Regul."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1042\/bj0920578","article-title":"The Isolation and Specific Activity of Rabbit-Muscle Glyceraldehyde Phosphate Dehydrogenase","volume":"92","author":"Ferdinand","year":"1964","journal-title":"Biochem. J."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1055\/s-2008-1025766","article-title":"Skeletal Muscle Enzyme Activities in Healthy Young Subjects","volume":"07","author":"Berg","year":"1986","journal-title":"Int. J. Sports Med."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1063\/1.555969","article-title":"Thermodynamics of Enzyme-Catalyzed Reactions: Part 4","volume":"24","author":"Goldberg","year":"1995","journal-title":"Lyases. J. Phys. Chem. Ref. Data"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1063\/1.555970","article-title":"Thermodynamics of Enzyme-Catalyzed Reactions: Part 5. Isomerases and Ligases","volume":"24","author":"Goldberg","year":"1995","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1016\/S0021-9258(18)91416-X","article-title":"A Kinetic Study of the Phosphoglucomutase Pathway","volume":"239","author":"Ray","year":"1964","journal-title":"J. Biol. Chem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/BF00585245","article-title":"NAD in Muscle of Man at Rest and during Exercise","volume":"376","author":"Graham","year":"1978","journal-title":"Pflug. Arch."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1007\/BF00584099","article-title":"NADH in Human Skeletal Muscle during Short-Term Intense Exercise","volume":"403","author":"Sahlin","year":"1985","journal-title":"Pfl\u00fcg. Arch. Eur. J. Physiol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1152\/jappl.1978.45.3.474","article-title":"Intracellular pH and Bicarbonate Concentration in Human Muscle during Recovery from Exercise","volume":"45","author":"Sahlin","year":"1978","journal-title":"J. Appl. Physiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2489","DOI":"10.1016\/S0021-9258(19)44135-5","article-title":"Glycolysis and the Permeation of Glucose and Lactate in the Isolated, Perfused Dog Brain during Anoxia and Postanoxic Recovery","volume":"248","author":"Drewes","year":"1973","journal-title":"J. Biol. Chem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1007\/BF02026706","article-title":"Triosephosphate Isomerase Deficiency: Haemolytic Anaemia, Myopathy with Altered Mitochondria and Mental Retardation Due to a New Variant with Accelerated Enzyme Catabolism and Diminished Specific Activity","volume":"150","author":"Eber","year":"1991","journal-title":"Eur. J. Pediatr."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1042\/bj1150837","article-title":"Disequilibrium in the Triose Phosphate Isomerase System in Rat Liver","volume":"115","author":"Veech","year":"1969","journal-title":"Biochem. J."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1093\/oxfordjournals.jbchem.a128240","article-title":"Studies on Erythrocyte Glycolysis I. Determination of the Glycolytic Intermediates in Human Erythrocytes","volume":"58","author":"Minakami","year":"1965","journal-title":"J. Biochem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1172\/JCI109129","article-title":"Human Erythrocyte Hexokinase Deficiency. Characterization of a Mutant Enzyme with Abnormal Regulatory Properties","volume":"62","author":"Rijksen","year":"1978","journal-title":"J. Clin. Investig."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1021\/bi00404a014","article-title":"Triosephosphate Isomerase Catalysis Is Diffusion Controlled. Appendix: Analysis of Triose Phosphate Equilibria in Aqueous Solution by Phosphorus-31 NMR","volume":"27","author":"Lim","year":"1988","journal-title":"Biochemistry"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/16\/7106\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T04:40:31Z","timestamp":1786423231000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/16\/7106"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,8]]},"references-count":106,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["ijms27167106"],"URL":"https:\/\/doi.org\/10.3390\/ijms27167106","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,8]]}}}