Nabeshima Takeshi, Kozaki Toshinori, Tomita Takashi, Kono Yoshiaki
Laboratory 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.
Biochem Biophys Res Commun. 2003 Jul 18;307(1):15-22. doi: 10.1016/s0006-291x(03)01101-x.
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.
从桃蚜（Myzus persicae）中分离出了编码两种乙酰胆碱酯酶（AChEs）的cDNA。MpAChE1与黑腹果蝇（Drosophila melanogaster）的ace基因直系同源，MpAChE2与黑腹果蝇的ace基因旁系同源。MpAChE1 cDNA推导的氨基酸序列在抗蚜威敏感和抗性品系之间是相同的。然而，在抗蚜威抗性品系中发现MpAchE2上存在Ser431Phe的单个氨基酸取代。该取代位于酶的酰基口袋中，被认为会改变配体特异性。
