Extensions to Michaelis-Menten Kinetics for Single Parameters.

Autor: Ariyawansha RTK; Postgraduate Institute of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka., Basnayake BFA; Postgraduate Institute of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka. benb@pdn.ac.lk.; Department of Agricultural Engineering, Faculty of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka. benb@pdn.ac.lk., Karunarathna AK; Postgraduate Institute of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka.; Department of Agricultural Engineering, Faculty of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka., Mowjood MIM; Postgraduate Institute of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka.; Department of Agricultural Engineering, Faculty of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2018 Nov 08; Vol. 8 (1), pp. 16586. Date of Electronic Publication: 2018 Nov 08.
DOI: 10.1038/s41598-018-34675-2
Abstrakt: Biochemical transformation kinetics is based on the formation of enzyme-substrate complexes. We developed a robust scheme based on unit productions of enzymes and reactants in cyclic events to comply with mass action law to form enzyme-substrate complexes. The developed formalism supports a successful application of Michaelis-Menten kinetics in all biochemical transformations of single parameters. It is an essential tool to overcome some challenging healthcare and environmental issues. In developing the formalism, we defined the substrate [S]= [Product] 3/4 and rate of reaction based on rate and time perspectives. It allowed us to develop two quadratic equations. The first, represents a body entity that gave a useful relationship of enzyme E = 2S 0.33 , and the second nutrients/feed, each giving [Enzymes] and [Enzyme-substrate complexes], simulating rate of reaction, [substrate], and their differentials. By combining [Enzymes] and [Enzyme-substrate complexes] values, this quadratic equation derives a Michaelis-Menten hyperbolic function. Interestingly, we can derive the proportionate rate of reaction and [Enzymes] values of the quadratics resulting in another Michaelis-Menten hyperbolic. What is clear from these results is that between these two hyperbolic functions, in-competitive inhibitions exist, indicating metabolic activities and growth in terms of energy levels. We validated these biochemical transformations with examples applicable to day to day life.
Databáze: MEDLINE
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