Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation of Leptinotarsa decemlineata

• DOI: 10.3390/ijms222111921
• Publication Date: 2021-11-03T21:59:38Z
• Authors: Yanjun Liu; Timothy Moural; Sonu Koirala B K; Jonathan Hernandez; Zhongjian Shen; Andrei Alyokhin; Fang Zhu
• Keywords: Xenobiotic; Glutathione S-transferase

Arthropod Glutathione S-transferases (GSTs) constitute a large family of multifunctional enzymes that are mainly associated with xenobiotic or stress adaptation. GST-mediated adaptation takes place through direct metabolism sequestration xenobiotics, and/or indirectly by providing protection against oxidative induced exposure. To date, the roles GSTs in Colorado potato beetle (CPB), notorious agricultural pest plants within Solanaceae, have not been well studied. Here, we functionally expressed and characterized an unclassified-class GST, LdGSTu1. The three-dimensional structure LdGSTu1 was solved resolution up to 1.8 Å X-ray crystallography. signature motif VSDGPPSL identified "G-site", it contains catalytically active residue Ser14. Recombinant used determine enzyme activity kinetic parameters using 1-chloro-2, 4-dinitrobenzene (CDNB), GSH, p-nitrophenyl acetate (PNA) as substrates. enzyme-substrate interaction studies demonstrated could catalyze conjugation GSH both CDNB PNA, higher turnover number for than PNA. inhibition assays enzymatic inhibited multiple pesticides, suggesting potential function