Literature DB >> 4062893

Analysis of progress curves for a highly concentrated Michaelian enzyme in the presence or absence of product inhibition.

N Kellershohn, M Laurent.   

Abstract

Methods are given for analysing the time course of an enzyme-catalysed reaction when the concentration of the enzyme itself is high, a situation which is often found in vivo. (1) The integrated form of the kinetic equation for a concentrated Michaelian enzyme in absence of product inhibition is given. Parameters are shown to be calculated easily using non-linear fitting procedures. (2) A general algorithm to analyse progress-curve data in more complex cases (i.e. when the analytical form of the integrated rate equation is not known or is exceedingly complex) is proposed. This algorithm may be used for any enzyme mechanism for which the differential form of the kinetic equation may be written analytically. We show that the method allows differentiation between the main types of product inhibition which may occur in the case of a highly concentrated Michaelian enzyme.

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Year:  1985        PMID: 4062893      PMCID: PMC1152704          DOI: 10.1042/bj2310065

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  12 in total

1.  [The biosynthesis of beta-galactosidase (lactase) in Escherichia coli; the specificity of induction].

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Journal:  FEBS Lett       Date:  1973-06-01       Impact factor: 4.124

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Review 6.  The statistical analysis of enzyme kinetic data.

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7.  Effect of enzyme concentration on the kinetics of D-lactate dehydrogenase from Aerobacter aerogenes.

Authors:  R V Sawula; I Suzuki
Journal:  Biochem Biophys Res Commun       Date:  1970-09-10       Impact factor: 3.575

8.  Use of integrated rate equations in estimating the kinetic constants of enzyme-catalyzed reactions.

Authors:  G W Schwert
Journal:  J Biol Chem       Date:  1969-03-10       Impact factor: 5.157

9.  In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. I. Catalytic and regulatory properties of aspartate transcarbamylase.

Authors:  B Penverne; G Hervé
Journal:  Arch Biochem Biophys       Date:  1983-09       Impact factor: 4.013

10.  A method for determining kinetic parameters at high enzyme concentrations.

Authors:  C J Halfman; F Marcus
Journal:  Biochem J       Date:  1982-04-01       Impact factor: 3.857

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  8 in total

1.  Progress-curve equations for reversible enzyme-catalysed reactions inhibited by tight-binding inhibitors.

Authors:  S E Szedlacsek; V Ostafe; R G Duggleby; M Serban; M O Vlad
Journal:  Biochem J       Date:  1990-02-01       Impact factor: 3.857

2.  Analysis of progress curves by simulations generated by numerical integration.

Authors:  C T Zimmerle; C Frieden
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857

3.  Analysis of progress curves for enzyme-catalysed reactions. Automatic construction of computer programs for fitting integrated rate equations.

Authors:  R G Duggleby; C Wood
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857

4.  A single-parameter family of adjustments for fitting enzyme kinetic models to progress-curve data.

Authors:  R G Duggleby; J C Nash
Journal:  Biochem J       Date:  1989-01-01       Impact factor: 3.857

5.  Progress-curve analysis in enzyme kinetics. Numerical solution of integrated rate equations.

Authors:  R G Duggleby
Journal:  Biochem J       Date:  1986-04-15       Impact factor: 3.857

6.  Prion diseases: dynamics of the infection and properties of the bistable transition.

Authors:  N Kellershohn; M Laurent
Journal:  Biophys J       Date:  2001-11       Impact factor: 4.033

7.  Modelling the effects of ageing time of starch on the enzymatic activity of three amylolytic enzymes.

Authors:  Nelson P Guerra; Lorenzo Pastrana Castro
Journal:  ScientificWorldJournal       Date:  2012-02-09

8.  Product inhibition of secreted phospholipase A2 may explain lysophosphatidylcholines' unexpected therapeutic properties.

Authors:  Timothy J Cunningham; Lihua Yao; Angel Lucena
Journal:  J Inflamm (Lond)       Date:  2008-10-22       Impact factor: 4.981

  8 in total

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