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

Microbiology/Biochemistry, INRS–Institut Armand-Frappier, Laval, Quebec, Canada
DOI
10.7287/peerj.preprints.3094v1
Subject Areas
Biochemistry, Computational Biology, Mathematical Biology, Drugs and Devices, Pharmacology
Keywords
Enzyme inhibition, Enzyme activation, Global data fitting, Model comparison, Drug development, Inhibition constant
Copyright
© 2017 Walsh
Licence
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
Cite this article
Walsh R. 2017. Comparing enzyme activity modifiers equations through the development of global data fitting templates in Excel. PeerJ Preprints 5:e3094v1

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]/Ki)). 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 previously reported enzyme kinetic data. This equation and the template developed in this article should prove to be useful tools in the study of enzyme inhibition and activation.

Author Comment

This is a submission to PeerJ for review.

Supplemental Information

S2 Inhibition of β-galactosidase by β-D-thiogalactopyranoside

DOI: 10.7287/peerj.preprints.3094v1/supp-2

S3 E. characias leave aq extract tyrosinase inhibitory activity

DOI: 10.7287/peerj.preprints.3094v1/supp-3

S4 E. characias leave EtOH extract tyrosinase inhibitory activity

DOI: 10.7287/peerj.preprints.3094v1/supp-4

S5 partial inhibition template

DOI: 10.7287/peerj.preprints.3094v1/supp-5

S6 modifier template alanine inhibition of glutamine synthase

DOI: 10.7287/peerj.preprints.3094v1/supp-6

S7 Partial inhibition template alanine inhibition of glutamine synthase

DOI: 10.7287/peerj.preprints.3094v1/supp-7

S8 modifier template inosine nucleosidase inhibition by adenine

DOI: 10.7287/peerj.preprints.3094v1/supp-8

S9 partial inhibition template inosine nucleosidase inhibition by adenine

DOI: 10.7287/peerj.preprints.3094v1/supp-9

S10 modifier template adenosine monophosphate inhibition of alcohol dehydrogenase

DOI: 10.7287/peerj.preprints.3094v1/supp-10

S11 partial inhibition template adenosine monophosphate inhibition of alcohol dehydrogenase

DOI: 10.7287/peerj.preprints.3094v1/supp-11

S12 modifier template adenosine triphosphate inhibition of mevalonate diphosphate decarboxylase

DOI: 10.7287/peerj.preprints.3094v1/supp-12

S13 partial inhibition template adenosine triphosphate inhibition of mevalonate diphosphate decarboxylase

DOI: 10.7287/peerj.preprints.3094v1/supp-13