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Biochem Biophys Res Commun. 2003 Jul 18;307(1):15-22.

An amino acid substitution on the second acetylcholinesterase in the pirimicarb-resistant strains of the peach potato aphid, Myzus persicae.

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  • 1Laboratory of Applied Zoology E407, Department of Agriculture and Forestry, Institute of Agriculture and Forestry, University of Tsukuba, Tennodai 1-1-1, Ibaraki, 305-8572, Japan.


cDNAs encoding two acetylcholinesterases (AChEs) were isolated from the peach potato aphid, Myzus persicae. MpAChE1 was orthologous and MpAChE2 was paralogous with the ace of Drosophila melanogaster. The deduced amino acid sequence of MpAChE1 cDNA was identical between the pirimicarb susceptible and resistant strains. However, a single amino acid substitution of Ser431Phe on MpAchE2 was found in the pirimicarb resistant strains. This substitution was located in the acyl pocket of the enzyme and was thought to alter the ligand specificity.

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