The scope, efficiency, and practicality of synthesizing chiral organic catalysts that simulate enzyme systems will be explored. Particular attention will be given to synthetic transacylases and reductases. In the transacylases, the substrates will be amino esters and amino amides. The alkylammonium ion complexing a macrocyclic polyether containing a nucleophile-leaving group and a chiral barrier will serve to collect and orient substrate and catalyst. In the reductases, a Zn2+ or NH4+ bound to a macrocyclic polyether containing a chiral barrier and an attached dihydropyridinium ion will bind and orient during reduction aldehydes and ketones. Particular attention will be given to asymmetric selection or synthesis in these synthetic catalysts. New rigid binding systems with convergent functional groups are being synthesized and tested.