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Thermodynamic analysis of enzyme catalysed reactions: new insights into the Michaelis–Menten equation

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A simple thermodynamic analysis of the well-known Michaelis-Menten equation (MME) of enzyme catalysis is proposed that employs the chemical potential μ to follow the Gibbs free energy changes attending the formation of the enzyme-substrate complex and its turnover to the product. The main conclusion from the above analysis is that low values of the Michaelis constant KM and high values of the turnover number kcat are advantageous: this supports a simple algebraic analysis of the MME, although at variance with current thinking. Available data apparently support the above findings. It is argued that transition state stabilisation—rather than substrate distortion or proximity—is the key to enzyme catalysis.

10.1163/15685670260188584
/content/journals/10.1163/15685670260188584
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/content/journals/10.1163/15685670260188584
2017-12-14

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