Abstract

The parameters in steady-state or rapid-equilibrium rate equations for enzyme-catalyzed reactions depend on the temperature, pH, and ionic strength, and may depend on the concentrations of specific species in the buffer. When the complete rate equation (i.e. the equation with parameters for the reverse reaction as well as the forward reaction) is determined, there are one or more Haldane relations between some of the kinetic parameters and the apparent equilibrium constant for the reaction that is catalyzed. When the apparent equilibrium constant can be calculated from the kinetic parameters, the equilibrium composition can be calculated. This is remarkable because the kinetic parameters all depend on the properties of the enzymatic site, but the apparent equilibrium constant and the equilibrium composition do not. The effects of ionic strength and pH on the unoccupied enzymatic site and the occupied enzymatic site have to cancel in the Haldane relation or in the calculation of the apparent equilibrium constant using the rate constants for the steps in the mechanism. Several simple enzymatic mechanisms and their complete rate equations are discussed.

Keywords: Kinetics of enzyme-catalyzed reactions; Rate equations; Haldane relations; Apparent equilibrium constants; Rate constants; Kinetic parameters

Article Outline

1. Introduction

2. Consideration of the effect of ionic strength on a simple mechanism

3. Consideration of the effect of pH on a simple mechanism

4. Inclusion of the pH-dependent reverse reaction

5. Consideration of the effects of pH on the rapid-equilibrium rate equation for the reaction A + B = P + Q

6. Expression of the apparent equilibrium constant for A + B = P + Q in terms of the rate constants of the steps in the forward and reverse direction

7. Discussion

Acknowledgements

References