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Comparing enzyme activity modifier equations through the development of global data fitting templates in Excel

Ryan Walsh 1, *
* Corresponding author
Abstract : The classical way of defining enzyme inhibition has obscured the distinction between inhibitory effect and the inhibitor binding constant. This article examines the relationship between the simple binding curve used to define biomolecular interactions and the standard inhibitory term (1 + ([I]∕K i )). By understanding how this term relates to binding curves which are ubiquitously used to describe biological processes, a modifier equation which distinguishes between inhibitor binding and the inhibitory effect, is examined. This modifier equation which can describe both activation and inhibition is compared to standard inhibitory equations with the development of global data fitting templates in Excel and via the global fitting of these equations to simulated and previously published datasets. In both cases, this modifier equation was able to match or outperform the other equations by providing superior fits to the datasets. The ability of this single equation to outperform the other equations suggests an over-complication of the field. This equation and the template developed in this article should prove to be useful tools in the study of enzyme inhibition and activation.
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Ryan Walsh. Comparing enzyme activity modifier equations through the development of global data fitting templates in Excel. PeerJ, PeerJ, 2018, 6, pp.e6082. ⟨10.7717/peerj.6082⟩. ⟨pasteur-02136231⟩

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