Enantioselective
Interaction of Acid α‑Naphthyl
Acetate Esterase with Chiral Organophosphorus Insecticides
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Abstract
Many previous works have demonstrated
that acetylcholinesterase
(AChE) was enantioselectively inhibited by chiral organophosphorus
insecticides (OPs) and that a significant difference in reactivation
existed for AChE inactivated by (1<i>R</i>)- versus (1<i>S</i>,3<i>S</i>)-stereoisomers of isomalathion. It
had been known that α-naphthyl acetate esterase (ANAE), an enzyme
which might play an essential role in the growth of plants and the
defense of plants against environmental stress by regulating the concentration
of hormones in plants, can be inhibited by OPs. However, it was unknown
whether interaction of ANAE with chiral OPs was enantioselective.
The present work investigated the inhibition kinetics and spontaneous
reactivation of ANAE inactivated by enantiomers of malaoxon, isomalathion,
and methamidophos. The order of inhibition potency is (<i>R</i>) > (<i>S</i>) for malaoxon, (1<i>R</i>,3<i>R</i>) > (1<i>R</i>,3<i>S</i>) > (1<i>S</i>,3<i>R</i>) > (1<i>S</i>,3<i>S</i>) for isomalathion, and (<i>S</i>) > (<i>R</i>) for methamidophos according to bimolecular rate constants
of inhibition
(<i>k</i><sub>i</sub>), which is consistent with the order
observed in the enantioselective inhibition of AChE by malaoxon, isomalathion,
and methamidophos. The difference in spontaneous reactivation of AChE
inactivated between (1<i>R</i>)- and (1<i>S</i>,3<i>S</i>)-isomers of isomalathion is conserved for ANAE.
The observations indicated ANAE and AChE have similar selective inhibition
kinetics and postinhibitory reactions in reaction with chiral OPs