Three structurally related haptens 1-3 were designed and synthesized with the goal of generating antibodies for the hydrolysis of ester 4a and amide 4b. These haptens contain a 1,2-amino alcohol functionality which replaces the ester/amide moiety of the substrates. A number of catalytic antibodies were generated, and the Michaelis-Menten kinetics constants of three representative catalytic antibodies induced to each of haptens 1-3 were determined. These catalytic antibodies accelerated the hydrolysis of ester 4a with k(cat)/k(un) = approximately 3 X 10(3), and their catalytic activities were effectively inhibited by the addition of their respective haptens. To evaluate the structural influences of the hapten on antibody binding and specificity as well as catalytic activity, a total of 18 antibodies including the above catalytic antibodies and three representative noncatalytic antibodies from each group were selected, and their dissociation constants with their respective haptens, amide 4b, and products were determined. The studies have shown that (1) the structural variations among the three haptens induce no significant changes in catalytic activity of antibodies while they slightly influence the antibody binding and specificity for the substrate and products and (2) a high probability (reaching nearly 50%) of finding catalytic activity among the monoclonal antibodies raised to hapten 1 is found, suggesting that the induction of a charged complementary amino acid residue in close proximity to the reaction site may be important to generation of catalytic antibodies.