Yamamoto Kohji, Hirowatari Aiko, Shiotsuki Takahiro, Yamada Naotaka
Kyushu University Graduate School, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan.
Institute of Agrobiological Sciences, NARO, Tsukuba, Ibaraki 305-8634, Japan.
J Pestic Sci. 2016 Nov 20;41(4):145-151. doi: 10.1584/jpestics.D16-048.
cDNA encoding an unclassified glutathione -transferase (GST) of the diamondback moth, , was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone was sequenced and the amino acid sequence deduced, revealing 67%-73% identities with unclassified GSTs from other organisms. A recombinant protein was functionally overexpressed in cells in a soluble form and purified to homogeneity. The enzyme was capable to catalyze the transformation of 1-chloro-2,4-dinitrobenzene and ethacrynic acid with glutathione. A competition assay revealed that GST activity was inhibited by insecticides, suggesting that the enzyme could contribute to insecticide metabolism in the diamondback moth.
通过逆转录聚合酶链反应克隆了编码小菜蛾一种未分类谷胱甘肽 -S-转移酶（GST）的cDNA。对所得克隆进行测序并推导氨基酸序列，结果显示与其他生物的未分类GST有67%-73%的同源性。一种重组蛋白在细胞中以可溶形式功能性过表达并纯化至同质。该酶能够催化谷胱甘肽与1-氯-2,4-二硝基苯和依他尼酸的转化。竞争试验表明GST活性受到杀虫剂抑制，这表明该酶可能在小菜蛾的杀虫剂代谢中发挥作用。
