Goličnik M (2012) On the Lambert W function and its utility in biochemical kinetics. Goličnik M (2011) Exact and approximate solutions for the decades-old Michaelis–Menten equation: progress-curve analysis through integrated rate equations.

Biochem J 139:715–720Įxnowitz F, Meyer B, Hackl T (2012) NMR for direct determination of K m and V max of enzyme reactions based on the Lambert W function-analysis of progress curves. A new graphical procedure for estimating enzyme kinetic parameters. Methods 24:168–174Įisenthal R, Cornish-Bowden A (1974) The direct linear plot. FEBS Lett 587:2725–2730ĭuggleby RG (2001) Quantitative analysis of the time courses of enzyme-catalyzed reactions. Berichte der Deutschen Chemischen Gesellschaft 30:117–124Ĭornish-Bowden A (2013) The origins of enzyme kinetics. J Chem Soc 81:373–388īuchner E (1897) Alcoholic fermentation without yeast cells. PLoS One 6:e22265īrown AJ (1902) Enzyme action. MATCH Commun Math Comput Chem 63:283–318īevc S, Konc J, Stojan J, Hodošček M, Penca M, Praprotnik M, Janežič D (2011) ENZO: a web tool for derivation and evaluation of kinetic models of enzyme catalyzed reactions. J Pharmacokinet Biopharm 10:109–119īerberan-Santos MN (2010) A general treatment of Henri–Michaelis–Menten enzyme kinetics: exact series solution and approximate analytical solutions. Kluwer, Bostonīeal SL (1982) On the solution to the Michaelis–Menten equation. However, a mathematical approach is reviewed here that might provide an alternative to the decades-old problem of data analysis of cholinesterase-catalyzed reactions, through the more complex Webb integrated rate equation.Īdomian G (1994) Solving frontier problems of physics: the decomposition method. 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 saturation-like hyperbolic behavior at high concentrations of charged substrates. 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. 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.

Graphpad prism 5 hyperbolic fit