Some observations on the chemical and stereochemical specificity of the de-alkylation of organophosphorus esters by a hepatic glutathione transferase.
Hepatic glutathione (GSH) S-methyl transferase from rabbit, pig and dog demethylates dimethyl phosphate triesters. No stereospecificity towards racemic ethyl methyl 2-chloro-1-(2,4-dichlorophenyl)vinyl phosphate could be demonstrated but the enzyme exhibited some selectivity towards the (+) and (-) forms of O-methyl S-methyl 1-naphthyl phosphorothiolate. Pig liver enzyme, purified 30-fold, demethylated th  prochiral substrate dimethyl 1-naphthyl phosphorothionate with 90% stero-selectivity.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004285:Dogs; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D009904:Optical Rotation; D009943:Organophosphorus Compounds / Q000378:metabolism*; D011817:Rabbits; D013045:Species Specificity; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013552:Swine
D009943:Organophosphorus Compounds; D005982:Glutathione Transferase