Catalysis of Phosphate by a Modified Polyethylenimine

During the past three decades,in order to mimic the action of serineproteases manymodel enzymes have been synthesized based on micellae,imidazole and polyethyleni-mines.In this note,we describe a new protease model which can(i)noncovalently bindester substrates,(ii)accept their phosphoryl groups and(iii)dephosporylate to regeneratethe original catalytic entity.It is a true catalyst.Model 1 possesses oxime groups and long hydrocarbon chains linked to amine nitro-gen of polyethylenimine.This polymer has some attractive features:(i)Being amphiphilic,1 forms intramolecular micellae which is capable of associating with esters and othersubstrates.(ii)It has very strong binding affinity for anions and marked esters.(iii)