PMID:15357291
| Citation |
Kim, YM, Park, K, Jung, SH, Choi, JH, Kim, WC, Joo, GJ and Rhee, IK (2004) Chlorothalonil-biotransformation by glutathione S-transferase of Escherichia coli. J. Microbiol. 42:42-6 |
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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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| Keywords |
Biotransformation; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Glutathione/metabolism; Glutathione Transferase/genetics; Glutathione Transferase/isolation & purification; Glutathione Transferase/metabolism; Nitriles/metabolism; Plasmids; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism |
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