Analysis of the substrate inhibition of complete and partial types

A simple graphical method was described for determining the kinetic parameters of substrate inhibition of complete and partial types. The method consists of plotting experimental data as \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \...

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Bibliographic Details
Main Authors: Yoshino, Masataka, Murakami, Keiko
Format: Online
Language:English
Published: Springer International Publishing 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4478191/
Description
Summary:A simple graphical method was described for determining the kinetic parameters of substrate inhibition of complete and partial types. The method consists of plotting experimental data as \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$v/\left( {V_{max} - v} \right)$$\end{document}v/Vmax-v versus the reciprocals of the substrate concentrations, where Vmax represents the maximal velocity. The reaction rate constant of enzyme–substrate–inhibitor complex \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$(k^{\prime } /k)$$\end{document}(k′/k) can be calculated from the ordinate intercept of the linear relationship between \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$v/\left( {V_{max} - v} \right)$$\end{document}v/Vmax-v and the reciprocal of the substrate concentrations at the higher and inhibitory concentrations of the substrate: partial type \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$(k^{\prime } /k < 1)$$\end{document}(k′/k<1) of the substrate inhibition gives straight lines intersecting with the ordinate at \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$(k^{\prime } /k)/( 1- k^{\prime } /k)$$\end{document}(k′/k)/(1-k′/k), whereas complete substrate inhibition \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$(k^{\prime } = 0)$$\end{document}(k′=0) yields straight lines converging on the origin. The \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$K_{i}^{\prime }$$\end{document}Ki′ value also can be calculated from the slope by using the \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$k^{\prime } /k$$\end{document}k′/k value determined. Validity of the method was confirmed by analyzing the substrate inhibition of phosphofructokinase II from E. coli. The present method provides a simple way for determining kinetic parameters of the substrate inhibition irrespective of complete and partial types.