Chandrasekhar, Sosale (2002) Thermodynamic analysis of enzyme catalysed reactions: new insights into the Michaelis-Menten equation. In: Research on Chemical Intermediates, 28 (4). pp. 265-275.
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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 mu 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 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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Springer.|
|Keywords:||Catalysis;chemical potential;enzyme;free energy;KM,kcat, Michaelis–Menten;thermodynamic.|
|Department/Centre:||Division of Chemical Sciences > Organic Chemistry|
|Date Deposited:||27 Jul 2011 07:47|
|Last Modified:||27 Jul 2011 07:47|
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