Open AccessDissection of enzymatic kinetics and elucidation of detailed parameters based on the Michaelis‐Menten model. Kinetic and thermodynamic connections
Author(s) -
Bonafe Carlos F. S.,
Lima Neto Daniel F.,
Aguirre César A. P.,
Vieira de Melo Silvio A. B.,
Lima Wallisson Dos S.,
Bispo Jose A. C.
Publication year - 2020
Publication title -
engineering reports
Language(s) - English
Resource type - Journals
ISSN - 2577-8196
DOI - 10.1002/eng2.12223
Subject(s) - michaelis–menten kinetics , chemistry , thermodynamics , kinetics , enzyme kinetics , kinetic energy , enzyme , activation energy , substrate (aquarium) , invertase , stereochemistry , enzyme assay , biochemistry , active site , physics , oceanography , quantum mechanics , geology
A computational procedure based on the numerical integration of the Michaelis‐Menten model of enzyme action, free of any restrictions of steady‐state conditions and substrate/enzyme ratios is proposed. The original Michaelis‐Menten data for invertase (Michaelis and Menten, 1913, Biochem Z. 49:333‐369) were reanalyzed. The surface and contour plots that were generated for substrate, free enzyme, complex, and product confirmed the model's usefulness. All energy potentials G and the “conformational drift parameter” δ involved in the enzymatic reactions were determined. Our findings indicate that at s o = 0.0052 M the enzyme‐substrate (ES) complex present an energy of dissociation of G E + S ➔ ES = 15.0 kJ/mol and as s o increases to 0.333 M, the G E + S ➔ ES value decreases to 5.0 kJ/mol, thereby decreasing its presence in solution. Overall, the ability to determine G and δ for each transition suggests a relationship between kinetics and thermodynamics. The analysis proposed here can be directly applied to chemical and biological situations, as well as industrial processes.