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Extensions to Michaelis-Menten Kinetics for Single Parameters
R T K Ariyawansha1, B F A Basnayake2,3, A K Karunarathna1,4
1Postgraduate Institute of Agriculture, University of Peradeniya, Peradeniya, 20400, Sri Lanka.
Scientific Reports
|November 10, 2018
Summary
This study introduces a new biochemical transformation formalism, extending Michaelis-Menten kinetics for enzyme-substrate complex formation. The model aids in addressing healthcare and environmental challenges through robust kinetic analysis.
Area of Science:
- Biochemistry
- Chemical Kinetics
Background:
- Biochemical transformations rely on enzyme-substrate complex formation.
- Existing models may face limitations in complex biological systems.
Purpose of the Study:
- To develop a robust formalism for biochemical transformation kinetics.
- To extend the application of Michaelis-Menten kinetics.
- To provide a tool for healthcare and environmental issue resolution.
Main Methods:
- Developed a scheme based on unit productions in cyclic events to form enzyme-substrate complexes.
- Defined substrate as [S] = [Product]^(3/4) and rate of reaction.
- Derived two quadratic equations to model enzyme-substrate dynamics and reaction rates.
Main Results:
- Established a relationship for enzyme: E = 2S^0.33.
- Simulated reaction rates, substrate concentrations, and differentials using quadratic equations.
- Derived Michaelis-Menten hyperbolic functions from combined enzyme and enzyme-substrate complex values.
- Identified in-competitive inhibitions between hyperbolic functions, indicating metabolic activity.
Conclusions:
- The developed formalism successfully applies Michaelis-Menten kinetics to biochemical transformations.
- The model provides insights into metabolic activities and growth.
- Validated with real-world applicable examples.
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