The use of two reverse self-assembling systems, such as reverse micelles and reverse vesicles, to model the enzymatic function of biological membranes is discussed. They permit direct measurement of enzyme kinetics since these ternary systems form optically transparent solutions. The physicochemical characteristics of both systems are differentiated since they clearly affect enzyme behavior. The four enzymatic profiles that have been described in reverse micelles as a function of micelle size (omega(0)) and the kinetic models developed to explain them are discussed. Reverse vesicles, first described in 1991, are also presented as a new system that shares properties with reverse micelles and liposomes, and in which enzymes show unexpected behavior. Finally, the potential use of these systems in protein extraction, hydrophobic protein stabilization, and biotechnology are noted, although a better physicochemical characterization is needed in order to explore their full potential.