title: A note on the kinetics of enzyme action: a decomposition that highlights thermodynamic effects.
abstract: Michaelis and Menten's mechanism for enzymatic catalysis is remarkable both in its simplicity and its wide applicability. The extension for reversible processes, as done by Haldane, makes it even more relevant as most enzymes catalyze reactions that are reversible in nature and carry in vivo flux in both directions. Here, we decompose the reversible Michaelis-Menten equation into three terms, each with a clear physical meaning: catalytic capacity, substrate saturation and thermodynamic driving force. This decomposition facilitates a better understanding of enzyme kinetics and highlights the relationship between thermodynamics and kinetics, a relationship which is often neglected. We further demonstrate how our separable rate law can be understood from different points of view, shedding light on factors shaping enzyme catalysis.
authors.affiliation: Department of Plant Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel. elad.noor@weizmann.ac.il
authors.forename: Elad
authors.initials: E
authors.lastname: Noor
authors.forename: Avi
authors.initials: A
authors.lastname: Flamholz
authors.forename: Wolfram
authors.initials: W
authors.lastname: Liebermeister
authors.forename: Arren
authors.initials: A
authors.lastname: Bar-Even
authors.forename: Ron
authors.initials: R
authors.lastname: Milo
mesh_terms: D000465:Algorithms; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D011485:Protein Binding; D013816:Thermodynamics
chemical_list: D004798:Enzymes
keywords: Enzyme kinetics; Michaelis–Menten; Reversible reaction; Thermodynamics