Abstract
The conceptual and practical issues regarding the reduction of the Haldane-Radić enzymic mechanism, specific for cholinesterase kinetics, to the consecrated or logistically modified Michaelis-Menten kinetics, specific for some mutant enzymes, are here clarified as due to the limited initial substrate concentration, through detailed initial rate and progress curve analysis, even when other classical conditions for such equivalence are not entirely fulfilled.
Highlights
Dating back more than a century since firstly proposed by Henri in 1901 [1] the generalMichaelis-Menten mechanism of enzyme kinetics (1913) [2] assumes that when an enzyme E acts upon a substrate S the complex ES is formed which in turn is converted into a product P and enzyme, according to Scheme 1 [3,4,5,6,7,8].Scheme 1
The present paper explores the temporal solution for the substrate traffic in the Haldane-Radić enzyme kinetics presented in Scheme 2 as it will be formulated either by closing WLambert analogously form of Equation (4) or even as analytical progress curves for identifying the cases its reduction to the Michaelis-Menten enzyme kinetics of Scheme 1 may be validated
While noting the persistent non-zero non-reactive behavior for higher substrate concentration – a feature that accounts for the inhibition character calling the Haldane specificity
Summary
Dating back more than a century since firstly proposed by Henri in 1901 [1] the general. Further variants of Scheme 2 were considered in regarding the modeling of inhibition of Drosophila melanogaster acetylcholinesterase active site gorge trying to furnish a putative model for the essentially not-Michaelis-Menten kinetics of cholinesterases in general, and those of insects in special, such that to combine activation and inhibition for a large range of substrate concentrations [2426] All these inhibition models originate into the classical Haldane equation [27]: Vmax [ S ]. The present paper explores the temporal solution for the substrate traffic in the Haldane-Radić enzyme kinetics presented in Scheme 2 as it will be formulated either by closing WLambert analogously form of Equation (4) or even as analytical progress curves for identifying the cases its reduction to the Michaelis-Menten enzyme kinetics of Scheme 1 may be validated
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