2019
DOI: 10.1142/s1793524519500086
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A much better replacement of the Michaelis–Menten equation and its application

Abstract: Michaelis-Menten equation is a basic equation of enzyme kinetics andgives an acceptable approximation of real chemical reaction processes. Analyzing the derivation of this equation yields the fact that its good performance of approximating real reaction processes is due to Michaelis-Menten curve (15). This curve is derived from Quasi-Steady-State Assumption(QSSA), which has been proved always true and called Quasi-Steady-State Law by Banghe Li et al [19].Here, we found a quartic equation A(S, E) = 0 (22), whic… Show more

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“…The Michaelis-Menten Curve is an indicator that can be used to describe changes in enzyme kinetics and to provide inhibitory characteristics for enzyme activity 19 . Km and Vmax values are two main parameters in the enzyme kinetics study, each of which represents the Michaelis-Menten constanta which can be used to estimate the number of substrates and acceleration reaction 20 .…”
Section: The Michaelis-menten Curvementioning
confidence: 99%
“…The Michaelis-Menten Curve is an indicator that can be used to describe changes in enzyme kinetics and to provide inhibitory characteristics for enzyme activity 19 . Km and Vmax values are two main parameters in the enzyme kinetics study, each of which represents the Michaelis-Menten constanta which can be used to estimate the number of substrates and acceleration reaction 20 .…”
Section: The Michaelis-menten Curvementioning
confidence: 99%