ArticlePloS one2014
Glutathione-binding site of a bombyx mori theta-class glutathione transferase.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Functional and Structural Diversity of Insect Glutathione S-transferases in Xenobiotic Adaptation.International journal of biological sciences · 2022Review
- Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice.Plant molecular biology · 2021Article
- Investigation of the Substrate-Binding Site of a Prostaglandin E Synthase in Bombyx mori.The protein journal · 2021Article
- Investigation of the active site of an unclassified glutathione transferase inJournal of pesticide science · 2020Article
- Transcriptome Sequencing of the Striped Cucumber Beetle,Biotech (Basel (Switzerland)) · 2020Article
- Article
- Characterisation of a diazinon-metabolising glutathione S-transferase in the silkworm Bombyx mori by X-ray crystallography and genome editing analysis.Scientific reports · 2018Article
- Biochemical characterization of an unclassified glutathioneJournal of pesticide science · 2016Article
- Identification of a diazinon-metabolizing glutathione S-transferase in the silkworm, Bombyx mori.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glutathione transferase (GST) superfamily plays key roles in the detoxification of various xenobiotics. Here, we report the isolation and characterization of a silkworm protein belonging to a previously reported theta-class GST family. The enzyme (bmGSTT) catalyzes the reaction of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and 4-nitrophenethyl bromide. Mutagenesis of highly conserved residues in the catalytic site revealed that Glu66 and Ser67 are important for enzymatic function. These results provide insights into the catalysis of glutathione conjugation in silkworm by bmGSTT and into the metabolism of exogenous chemical agents.
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Registered trials
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