Kinetics of allosteric activation

Although enzyme inhibition results in most cases from the competing effect of a ligand with substrate, the ability of ligands to enhance enzyme function requires binding to a site distinct from the active site. This is the basis of allosteric activation of enzyme activity, documented most conspicuously in the vast family of enzymes activated by monovalent cations. In this chapter, we review the basic kinetic aspects of allosteric activation by taking into consideration the biologically relevant case of an enzyme E possessing a single site for substrate S and a single site for the allosteric effector L.