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To test this, we quantified the absolute concentrations of glycolytic enzymes in three bacterial species\u2014\n                      <jats:italic toggle=\"yes\">Zymomonas mobilis<\/jats:italic>\n                      ,\n                      <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                      , and\n                      <jats:italic toggle=\"yes\">Clostridium thermocellum<\/jats:italic>\n                      \u2014which employ distinct glycolytic pathways with varying thermodynamic driving forces. By integrating enzyme concentration data with corresponding\n                      <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                      metabolic fluxes and \u0394\n                      <jats:italic toggle=\"yes\">G<\/jats:italic>\n                      measurements, we found that the highly favorable Entner-Doudoroff pathway in\n                      <jats:italic toggle=\"yes\">Z. mobilis<\/jats:italic>\n                      requires only one-fourth the amount of enzymatic protein to sustain the same flux as the thermodynamically constrained pyrophosphate-dependent glycolytic pathway in\n                      <jats:italic toggle=\"yes\">C. thermocellum<\/jats:italic>\n                      , with the Embden-Meyerhof-Parnas pathway in\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      exhibiting intermediate thermodynamic favorability and enzyme demand. Across all three pathways, early reactions with stronger thermodynamic driving forces generally required lower enzyme investment than later, less favorable steps. Additionally, reflecting differences in glycolytic strategies, the highly reversible ethanol fermentation pathway in\n                      <jats:italic toggle=\"yes\">C. thermocellum<\/jats:italic>\n                      requires 10-fold more protein to maintain the same flux as the irreversible, forward-driven ethanol fermentation pathway in\n                      <jats:italic toggle=\"yes\">Z. mobilis<\/jats:italic>\n                      . Thus, protein investment across glycolytic pathways reflects differences in their thermodynamic favorability.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Cells regulate metabolic fluxes to balance energy production, biosynthesis, and the efficient use of limited resources, including the finite capacity for synthesizing and maintaining metabolic enzymes. Here, we present\n                        <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                        evidence that strongly thermodynamically favorable metabolic pathways require significantly fewer enzyme resources to sustain a given flux compared to less thermodynamically favorable pathways. These findings underscore the connection between pathway thermodynamics, resource allocation, and enzyme burden, providing valuable insights for metabolic engineering strategies aimed at optimizing pathways for high flux with minimal protein cost.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.01837-25","type":"journal-article","created":{"date-parts":[[2025,9,16]],"date-time":"2025-09-16T13:00:36Z","timestamp":1758027636000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["Thermodynamics shapes the\n                    <i>in vivo<\/i>\n                    enzyme burden of glycolytic pathways"],"prefix":"10.1128","volume":"16","author":[{"given":"Daven B.","family":"Khana","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01e4byj08","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Bacteriology, 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