Enzymes involved in the detoxification of organophosphorus, carbamate and pyrethroid insecticides through hydrolysis

Abstract

The most employed insecticides for indoor and agriculture purposes belong to carbamates, pyrethroid or organophosphates. The chemical structures of these three groups correspond to carbamic, carboxylic and triphosphoric esters. Technical monographs suggest that the hydrolysis of ester bonds of carbamates and pyrethroids plays an important role in the detoxification of these compounds. However, detailed studies about enzymes hydrolysing carbamates and pyrethroids in vertebrates are not available. Certain carbamate hydrolysing activities are associated to serum albumin. Phosphotriesterases, being of an unknown physiological role, hydrolyse (in some cases stereospecifically) organophosphorus insecticides (OP). Phosphotriesterases have been found in a multitude of species, from mammals to bacteria. A phosphotriesterase activity, EDTA-resistant, has been detected in serum albumin. Phosphotriesterases in serum of mammals display polymorphisms. Phosphotriesterases offer applications in therapy of organophosphorus poisonings, in biodegradation and bioremedation of organophosphates. Similar studies should be developed with enzymes hydrolysing pyrethroids and carbamate insecticides. Such studies will improve the knowledge of the detoxification routes in non-target species and will help to design specific and safer carbamate and pyrethroid insecticides.