A note on the kinetics of enzyme action: A decomposition that highlights thermodynamic effects

Elad Noor, Avi Flamholz, Wolfram Liebermeister, Arren Bar-Even, Ron Milo

Research output: Contribution to journalReview articlepeer-review

59 Scopus citations

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.

Original languageEnglish
Pages (from-to)2772-2777
Number of pages6
JournalFEBS Letters
Volume587
Issue number17
DOIs
StatePublished - 2 Sep 2013
Externally publishedYes

Keywords

  • Enzyme kinetics
  • Michaelis-Menten
  • Reversible reaction
  • Thermodynamics

Fingerprint

Dive into the research topics of 'A note on the kinetics of enzyme action: A decomposition that highlights thermodynamic effects'. Together they form a unique fingerprint.

Cite this