A note on the kinetics of enzyme action: A decomposition that highlights thermodynamic effects. Issue 17 (23rd July 2013)

• Record Type: Journal Article
• Authors: Noor, Elad; Flamholz, Avi; Liebermeister, Wolfram; Bar-Even, Arren; Milo, Ron
• Is Part Of: FEBS letters. Volume 587:Issue 17(2013)
• Page Start: 2772
• Page End: 2777
• Publication Date: 2013-07-23
• Subjects: Enzyme kinetics -- Thermodynamics -- Michaelis–Menten -- Reversible reaction; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.07.028
• Languages: English
• ISSNs: 0014-5793

Abstract

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.