Probing the active sites of butyrylcholinesterase and cholesterol esterase with isomalathion: conserved stereoselective inactivation of serine hydrolases structurally related to acetylcholinesterase.
作者： Jonathan A. Doorn , Todd T. Talley , Charles M. Thompson , Rudy J. Richardson
DOI: 10.1021/TX015501S
关键词:
摘要: Previous work has shown that acetylcholinesterase (AChE), a member of the α/β-hydrolase superfamily, is stereoselectively inhibited by four stereoisomers isomalathion. Recent kinetic and mass spectral data demonstrated difference in mechanism inactivation exists for AChE treated with (1R)- versus (1S,3S)-stereoisomers. This study sought to determine whether other α/β-hydrolases are isomalathion if between (1S,3S)-isomers conserved α/β-hydrolases. Bimolecular rate constants inhibition (ki) were measured human equine butyrylcholinesterase (HBChE EBChE, respectively) bovine cholesterol esterase (BCholE) all isomers. Isomalathion isomers these enzymes following order potency: (1R,3R) > (1R,3S) (1S,3R) ≥ (1S,3S). Ratios ki values most potent least isomer 10.5 (HBChE), 11.9 (EBChE), 68.6 (BCholE). Rate ...
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