These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A note on the kinetics of enzyme action: a decomposition that highlights thermodynamic effects.
    Author: Noor E, Flamholz A, Liebermeister W, Bar-Even A, Milo R.
    Journal: FEBS Lett; 2013 Sep 02; 587(17):2772-7. PubMed ID: 23892083.
    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.
    [Abstract] [Full Text] [Related] [New Search]