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

ABSTRACT: 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.

SUBMITTER: Yamamoto K

PROVIDER: S-EPMC6140639 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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

Yamamoto Kohji K Hirowatari Aiko A Shiotsuki Takahiro T Yamada Naotaka N

Journal of pesticide science 20161101 4

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 th ...[more]

PMID: 30363080

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