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

Thermodynamic analysis of enzyme catalysed reactions: new insights into the Michaelis–Menten... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Research on Chemical Intermediates Springer Journals

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

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Publisher
Brill Academic Publishers
Copyright
Copyright © 2002 by VSP 2002
Subject
Chemistry; Inorganic Chemistry; Physical Chemistry; Catalysis
ISSN
0922-6168
eISSN
1568-5675
D.O.I.
10.1163/15685670260188584
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Research on Chemical IntermediatesSpringer Journals

Published: Oct 13, 2004

References

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