Abstract
In 1946, Linus Pauling argued that an enzyme derives its catalytic power by binding the transition state of a reaction more tightly than either its substrates or products. Thus, the active site of an enzyme lowers the energy barrier of the reaction and thereby increases the reaction rate. In 1969, Jencks suggested that an antibody, raised against a stable transition state analog of a reaction, should act as a potent catalyst. Since 1986, the vast repertoire of the immune system has been exploited for the generation of tailor-made biological catalysts. A number of strategies have been developed to generate catalytic antibodies that carry out a wide range of reactions with exquisite specificities.