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The properties of a carboxyl esterase from the peach potato aphid myzus persicae and its role in conferring insecticide resistance



The properties of a carboxyl esterase from the peach potato aphid myzus persicae and its role in conferring insecticide resistance



Biochemical Journal 167(3): 675-684



Carboxylesterase from different strains of M. persicae were examined to try to understand their contribution to insecticide resistance. Preliminary evidence that they are involved comes from the good correlation between the degree of resistance and the carboxylesterase and paraoxon-degrading activity in aphid homogenates. Carboxylesterase associated with resistance could not be separated from the insecticide-degrading enzyme by electrophoresis or ion-exchange chromatography. Homogenates of resistant aphids hydrolyzed paraoxon 60 times faster than those of susceptible aphids, yet the purified enzymes from both sources had identical catalytic-center activities towards this substrate and towards naphth-1-yl acetate, the latter being hydrolyzed by both 2 .times. 106 times faster than paraoxon. The enzyme from both sources is identical; one enzyme hydrolyzes both substrates. This was confirmed by relating the rate of paraoxon hydrolysis to the rate at which paraoxon-inhibited carboxylesterase re-activated. Both had the same 1st-order rate constant (0.01 min-1), showing clearly that the hydrolysis of both substrates is brought about by the same enzyme. Km for naphth-1-yl acetate was 0.131 mM, and for paraoxon 75 pM. The latter very small value could not be measured directly, but was calculated from substrate-competition studies coupled with measurements of re-activation of the diethyl phosphorylated enzyme. Since the purified enzymes from resistant and susceptible aphids had the same catalytic-center activity, the 60-fold difference between strains must be caused by different amounts of the same enzyme resulting from mutations of the regulator gene(s) rather than of the structural gene.

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