Selon le modèle de Michaelis et Menten, l'équation décrivant la vitesse initiale stationnaire d'une réaction enzymatique est la suivante : Avec : v i {\displaystyle v_ {i}} : vitesse initiale (c'est-à-dire en absence de produit) stationnaire (indépendante du temps) de la réaction enzymatique pour une concentration initiale en substrat.. The Michaelis-Menten kinetics equation includes two key terms: Maximum reaction rate, or V max, occurs when all substrate binding sites in an enzyme are full. Michaelis constant or K m, is the concentration of substrate at which the reaction rate is half of its maximum value (V max).The K m value indicates how well an enzyme is able to perform its activity at different concentrations of its.

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Michaelis and Menten equation (MM equation) has dominated biochemistry for more than a century after its seminal introduction in a paper published in 1913 in the journal Biochemische Zeitschrift, a predecessor of FEBS Journal [[]].Hence, publishing this guide in FEBS Journal would represent an apt dedication to the unmatched service rendered by this journal to the scientific community for more.. The Michaelis-Menten analysis incorporates the additional assumption that k 2 is much less than k-1,. A. R. Fersht, 1988, pp98-101. The rate equation can be integrated in two ways: Approximation I: Re-introducing the assumption that [E] is small, set [A] = [A] 0 - [C]. The Briggs-Haldane equation can now be integrated: