Thermodynamics shape the <i>in vivo</i> enzyme burden of glycolytic pathways.

ABSTRACT: Thermodynamically constrained reactions and pathways are hypothesized to impose greater protein demands on cells, requiring higher enzyme amounts to sustain a given flux compared to those with stronger thermodynamics. To test this, we quantified the absolute concentrations of glycolytic enzymes in three bacterial species -Zymomonas mobilis, Escherichia coli, and Clostridium thermocellum- which employ distinct glycolytic pathways with varying thermodynamic driving forces. By integrating enzyme concentration data with corresponding in vivo metabolic fluxes and ΔG measurements, we found that the highly favorable Entner-Doudoroff (ED) pathway in Z. mobilis requires only one-fourth the amount of enzymatic protein to sustain the same flux as the thermody

SUBMITTER: Khana DB 

PROVIDER: S-EPMC11838459 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature