Glutathione-S-transferases (GSTs; EC 2.5.1.18) are multifunctional proteins involved in plant detoxification processes. GSTs catalyze the conjugation of xenobiotics with the tripeptide glutathione (GSH). In
Arabidopsis thaliana there are 55 GST members known. To characterize these GSTs a heterologous test system was established in
Saccharomyces cerevisiae. Exposed to xenobiotic stress expressions of Arabidopsis GSTs were sugar-dependent induced in GST-deficient yeast mutant strains. Using high-resolution mass spectrometry (ICR-FT/MS), HPLC, and stabile isotope labeling pesticides were screened for GST/GSH-dependent biotransformation. Herbicide safeners and fungicides, e.g. anilazine, were substrate-specific S-glutathionylated by Arabidopsis GSTs. For the first time analysis demonstrated a broad detoxification function of phi-class GSTs against xenobiotics.
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Glutathione-S-transferases (GSTs; EC 2.5.1.18) are multifunctional proteins involved in plant detoxification processes. GSTs catalyze the conjugation of xenobiotics with the tripeptide glutathione (GSH). In
Arabidopsis thaliana there are 55 GST members known. To characterize these GSTs a heterologous test system was established in
Saccharomyces cerevisiae. Exposed to xenobiotic stress expressions of Arabidopsis GSTs were sugar-dependent induced in GST-deficient yeast mutant strains. Using high-...
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