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A different view of Henri-Michaelis-Menten (HMM) enzyme kinetics is presented. In the first part of the paper, a simplified but useful description that stresses the cyclic nature of the catalytic process is introduced. The time-dependence of the substrate concentration after the initial transient phase is derived in a simple way that dispenses the mathematical technique known as quasi-steady-state approximation. In the second part of the paper an exact one-dimensional formulation of HMM kinetics is obtained. The whole problem is condensed in a single one-variable evolution equation that is a second-order non-linear differential equation, and the control parameters are reduced to three dimensionless quantities: enzyme efficiency, substrate reduced initial concentration, and enzyme reduced initial concentration. The exact solution of HMM kinetics is obtained as a set of Maclaurin series. From the same equation, a number of approximate solutions, some known, some new, are derived in a systematic way that allows a precise evaluation of the respective level of approximation and conditions of validity. The evolution equation derived is also shown to be well suited for the numerical compu

Author

Berberan-Santos, Mario N.

Published

2009

Language

EN