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 K M and high values of the turnover number k cat 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.
Research on Chemical Intermediates – Springer Journals
Published: Oct 13, 2004
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