Biochemical characterization of an unclassified glutathione S-transferase of Plutella xylostella

cDNA encoding an unclassified glutathione S-transferase (GST) of the diamondback moth, Plutella xylostella, 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 o...

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Bibliographic Details
Published in:Journal of Pesticide Science 2016/11/20, Vol.41(4), pp.145-151
Main Authors: Yamamoto, Kohji, Hirowatari, Aiko, Shiotsuki, Takahiro, Yamada, Naotaka
Format: Article
Language:English
Subjects:
1-Chloro-2,4-dinitrobenzene
Agrochemicals
Amino acid sequence
Assaying
Biochemistry
Competition
Complementary DNA
Dinitrobenzene
E coli
Enzymes
Ethacrynic acid
Genes
Glutathione
Glutathione transferase
Homogeneity
Insecticides
Lepidoptera
Metabolism
Original
Plutella xylostella
Polymerase chain reaction
RNA-directed DNA polymerase
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Summary:cDNA encoding an unclassified glutathione S-transferase (GST) of the diamondback moth, Plutella xylostella, 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 Escherichia coli 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.
ISSN:1348-589X
1349-0923
DOI:10.1584/jpestics.D16-048