Chlorothalonil-biotransformation by glutathione S-transferase of Escherichia coli |
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Authors: | Kim Young-Mog Park Kunbawui Jung Soon-Hyun Choi Jun-Ho Kim Won-Chan Joo Gil-Jae Rhee In-Koo |
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Affiliation: | Institute of Agricultural Science & Technology , Kyungpook National University, Daegu 702-701, Korea. |
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Abstract: | It has recently been reported that one of the most important factors of yeast resistance to the fungicide chlorothalonil is the glutathione contents and the catalytic efficiency of glutathione S-transferase (GST) (Shin et al, 2003). GST is known to catalyze the conjugation of glutathione to a wide variety of xenobiotics, resulting in detoxification. In an attempt to elucidate the relation between chlorothalonil-detoxification and GST, the GST of Escherichia coli was expressed and purified. The drug-hypersensitive E. coli KAM3 cells harboring a plasmid for the overexpression of the GST gene can grow in the presence of chlorothalonil. The purified GST showed chlorothalonil-biotransformation activity in the presence of glutathione. Thus, chlorothalonil is detoxified by the mechanism of glutathione conjugation catalyzed by GST. |
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