[Interaction of bis-phosphorylated methanes with mammalian esterases].
The interaction of human erythrocyte acetylcholinesterase, horse serum butyrylcholinesterase and rat liver carboxylesterase with insecticides (RO)2P(O)SCH(COOEt)SP(O)(OR)2 (I) and (RO)2P(O)SCH(COOEt)OP(S)(OR)2 (II) was studied. The type I and II compounds were not hydrolyzed by carboxylesterase and inhibited the esterases irreversibly. A complex pattern of inhibition of acetylcholinesterase and butyrylcholinesterase by these compounds was caused by kinetically-manifested formation of an enzyme-inhibitor complex. The compounds I and II were more selective towards butyrylcholinesterase than towards acetylcholinesterase and carboxylesterase (kII two orders of magnitude higher) because of effective binding in the butyrylcholinesterase active center (K alpha 10(-8)--10(-9) M) due to hydrophobic interaction. An important role of the thion-phosphoryl-containing fragment in the interaction of type II compounds with hydrophobic sites of butyrylcholinesterase and carboxylesterase active centers was established.
D000110:Acetylcholinesterase / Q000097:blood; D000818:Animals; D002091:Butyrylcholinesterase / Q000097:blood; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors; D055598:Chemical Phenomena; D002621:Chemistry; D002800:Cholinesterase Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D004912:Erythrocytes / Q000201:enzymology; D006736:Horses; D006801:Humans; D007306:Insecticides / Q000138:chemical synthesis* / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009946:Organothiophosphorus Compounds; D051381:Rats
D002800:Cholinesterase Inhibitors; D007306:Insecticides; D009946:Organothiophosphorus Compounds; D002265:Carboxylic Ester Hydrolases; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase
Vzaimodeĭstvie bisfosforilirovannykh metanov s ésterazami mlekopitaiushchikh.