Abstract
A rate equation (or the rate law) gives the experimentally observed dependence of rate on the concentration of reactants. Rate equations are at the heart of any kinetic study as they help us describe the system in a mathematical formalism. This is true for enzyme catalysis as well. Besides its aesthetic beauty, the compact mathematical description of reaction kinetics serves the twin purposes of qualitative description of the system and quantitative evaluation of rate constants. An early attempt to capture the kinetics of enzyme catalysis was made by Victor Henri (in 1903, Chap. 2), and this was subsequently developed by Leonor Michaelis and Maud Menten (in 1913). The rate equation so described is a fundamental equation of enzyme kinetics and goes by the name Henri–Michaelis–Menten equation. It is more commonly referred to as Michaelis–Menten equation. The derivation of the rate equation for a simple, single-substrate enzymatic reaction is especially instructive. In the process, it describes the general logic used to derive such rate equations – an exercise central to any enzyme kinetic study. This chapter will describe the development, significance, and salient features of the Michaelis–Menten equation.
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Suggested Reading
Johnson KA (2013) A century of enzyme kinetic analysis, 1913 to 2013. FEBS Lett 587:2753–2766 part of Historical perspectives: special issue on the occasion of the centenary of the Michaelis-Menten paper
Johnson KA, Goody RS (2011) The original Michaelis constant: translation of the 1913 Michaelis-Menten paper. Biochemistry 50:8264–8269
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Punekar, N.S. (2018). Henri–Michaelis–Menten Equation. In: ENZYMES: Catalysis, Kinetics and Mechanisms. Springer, Singapore. https://doi.org/10.1007/978-981-13-0785-0_15
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DOI: https://doi.org/10.1007/978-981-13-0785-0_15
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