Literature DB >> 24078521

Progress-curve analysis through integrated rate equations and its use to study cholinesterase reaction dynamics.

Marko Goličnik.   

Abstract

Michaelis and Menten found the direct mathematical analysis of their studied enzyme-catalyzed reaction unrealistic 100 years ago, and hence, they avoided this problem by correct adaptation and analysis of the experiment, i.e., differentiation of the progress-curve data into rates. However, the most elegant and ideal simplification of the evaluation of kinetics parameters from progress curves can be performed when the algebraic integration of the rate equation results in an explicit mathematical equation that describes the dynamics of the model system of the reaction. Recently, it was demonstrated that such an alternative approach can be considered for enzymes that obey the generalized Michaelis–Menten reaction dynamics, although its use is now still limited for cholinesterases, which show kinetics that deviate from saturationlike hyperbolic behavior at high concentrations of charged substrates. However, a mathematical approach is reviewed here that might provide an alternative to the decades-old problemof data analysis of cholinesterase-catalyzed reactions, through the more complex Webb integrated rate equation.

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Year:  2014        PMID: 24078521     DOI: 10.1007/s12031-013-0129-y

Source DB:  PubMed          Journal:  J Mol Neurosci        ISSN: 0895-8696            Impact factor:   3.444


  16 in total

1.  NMR for direct determination of K(m) and V(max) of enzyme reactions based on the Lambert W function-analysis of progress curves.

Authors:  Franziska Exnowitz; Bernd Meyer; Thomas Hackl
Journal:  Biochim Biophys Acta       Date:  2011-10-29

2.  The integrated Michaelis-Menten rate equation: déjà vu or vu jàdé?

Authors:  Marko Goličnik
Journal:  J Enzyme Inhib Med Chem       Date:  2012-05-28       Impact factor: 5.051

Review 3.  The origins of enzyme kinetics.

Authors:  Athel Cornish-Bowden
Journal:  FEBS Lett       Date:  2013-06-19       Impact factor: 4.124

4.  Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase.

Authors:  P Masson; P Legrand; C F Bartels; M T Froment; L M Schopfer; O Lockridge
Journal:  Biochemistry       Date:  1997-02-25       Impact factor: 3.162

5.  The original Michaelis constant: translation of the 1913 Michaelis-Menten paper.

Authors:  Leonor Michaelis; Maud Leonora Menten; Kenneth A Johnson; Roger S Goody
Journal:  Biochemistry       Date:  2011-09-09       Impact factor: 3.162

6.  Exact and approximate solutions for the decades-old Michaelis-Menten equation: Progress-curve analysis through integrated rate equations.

Authors:  Marko Goličnik
Journal:  Biochem Mol Biol Educ       Date:  2011 Mar-Apr       Impact factor: 1.160

7.  The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters.

Authors:  R Eisenthal; A Cornish-Bowden
Journal:  Biochem J       Date:  1974-06       Impact factor: 3.857

8.  On the solution to the Michaelis-Menten equation.

Authors:  S L Beal
Journal:  J Pharmacokinet Biopharm       Date:  1982-02

9.  Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors.

Authors:  Z Radić; N A Pickering; D C Vellom; S Camp; P Taylor
Journal:  Biochemistry       Date:  1993-11-16       Impact factor: 3.162

10.  Strategies to resolve the catalytic mechanism of acetylcholinesterase.

Authors:  Terrone L Rosenberry
Journal:  J Mol Neurosci       Date:  2010-01       Impact factor: 3.444

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