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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| Format: | Online |
| Language: | English |
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Springer International Publishing
2015
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4478191/ |
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pubmed-4478191 |
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oai_dc |
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pubmed-44781912015-06-26 Analysis of the substrate inhibition of complete and partial types Yoshino, Masataka Murakami, Keiko Research 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. Springer International Publishing 2015-06-24 /pmc/articles/PMC4478191/ /pubmed/26120509 http://dx.doi.org/10.1186/s40064-015-1082-8 Text en © Yoshino and Murakami. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Yoshino, Masataka Murakami, Keiko |
| spellingShingle |
Yoshino, Masataka Murakami, Keiko Analysis of the substrate inhibition of complete and partial types |
| author_facet |
Yoshino, Masataka Murakami, Keiko |
| author_sort |
Yoshino, Masataka |
| title |
Analysis of the substrate inhibition of complete and partial types |
| title_short |
Analysis of the substrate inhibition of complete and partial types |
| title_full |
Analysis of the substrate inhibition of complete and partial types |
| title_fullStr |
Analysis of the substrate inhibition of complete and partial types |
| title_full_unstemmed |
Analysis of the substrate inhibition of complete and partial types |
| title_sort |
analysis of the substrate inhibition of complete and partial types |
| description |
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. |
| publisher |
Springer International Publishing |
| publishDate |
2015 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4478191/ |
| _version_ |
1613239374004092928 |