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• W1993854668 endingPage "e1004195" @default.
• W1993854668 startingPage "e1004195" @default.
• W1993854668 abstract "Kinetic models provide the means to understand and predict the dynamic behaviour of enzymes upon different perturbations. Despite their obvious advantages, classical parameterizations require large amounts of data to fit their parameters. Particularly, enzymes displaying complex reaction and regulatory (allosteric) mechanisms require a great number of parameters and are therefore often represented by approximate formulae, thereby facilitating the fitting but ignoring many real kinetic behaviours. Here, we show that full exploration of the plausible kinetic space for any enzyme can be achieved using sampling strategies provided a thermodynamically feasible parameterization is used. To this end, we developed a General Reaction Assembly and Sampling Platform (GRASP) capable of consistently parameterizing and sampling accurate kinetic models using minimal reference data. The former integrates the generalized MWC model and the elementary reaction formalism. By formulating the appropriate thermodynamic constraints, our framework enables parameterization of any oligomeric enzyme kinetics without sacrificing complexity or using simplifying assumptions. This thermodynamically safe parameterization relies on the definition of a reference state upon which feasible parameter sets can be efficiently sampled. Uniform sampling of the kinetics space enabled dissecting enzyme catalysis and revealing the impact of thermodynamics on reaction kinetics. Our analysis distinguished three reaction elasticity regions for common biochemical reactions: a steep linear region (0> ΔGr >-2 kJ/mol), a transition region (-2> ΔGr >-20 kJ/mol) and a constant elasticity region (ΔGr <-20 kJ/mol). We also applied this framework to model more complex kinetic behaviours such as the monomeric cooperativity of the mammalian glucokinase and the ultrasensitive response of the phosphoenolpyruvate carboxylase of Escherichia coli. In both cases, our approach described appropriately not only the kinetic behaviour of these enzymes, but it also provided insights about the particular features underpinning the observed kinetics. Overall, this framework will enable systematic parameterization and sampling of enzymatic reactions." @default.
• W1993854668 created "2016-06-24" @default.
• W1993854668 creator A5061172047 @default.
• W1993854668 creator A5067817255 @default.
• W1993854668 date "2015-04-14" @default.
• W1993854668 modified "2023-10-15" @default.
• W1993854668 title "A General Framework for Thermodynamically Consistent Parameterization and Efficient Sampling of Enzymatic Reactions" @default.
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• W1993854668 doi "https://doi.org/10.1371/journal.pcbi.1004195" @default.
• W1993854668 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4397067" @default.
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• W1993854668 hasPublicationYear "2015" @default.
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