It has been known for at least 20 years that monomeric enzymes can in principle show kinetic behaviour similar in appearance to the binding of ligands to oligomeric proteins in which there are co-operative interactions between multiple binding sites. However, the initial lack of experimental examples of kinetic co-operativity suggested that in nature co-operativity always arose from interactions between binding sites. Now, however, several examples are known, most of which cannot be explained in terms of multiple binding sites on one polypeptide chain. All current theoretical models for monomeric co-operativity postulate that it arises from the presence in the mechanism of parallel pathways for substrate binding that are slow compared with the possible rate of the catalytic reaction. Rapid removal of the intermediates produced in the slow steps prevents them from approaching equilibrium and allows the appearance of kinetic properties that would not be possible in systems at equilibrium.