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• W2899322032 abstract "Abstract 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 = 2 S 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." @default.
• W2899322032 created "2018-11-09" @default.
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• W2899322032 date "2018-11-08" @default.
• W2899322032 modified "2023-10-12" @default.
• W2899322032 title "Extensions to Michaelis-Menten Kinetics for Single Parameters" @default.
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• W2899322032 doi "https://doi.org/10.1038/s41598-018-34675-2" @default.
• W2899322032 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6224567" @default.
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• W2899322032 hasPublicationYear "2018" @default.
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