Chlorothalonil- Biotransformation by Glutathione S- Transferase of Escherichia coli

  • Kim, Young-Mog (Institute of Agricultural Science & Technology) ;
  • Park, Kunbawui (Department of Agricultural Chemistry, Kyungpook National Universit) ;
  • Jung, Soon-Hyun (Department of Agricultural Chemistry, Kyungpook National Universit) ;
  • Park, Jun-Ho (Department of Agricultural Chemistry, Kyungpook National Universit) ;
  • Kim, Won-Chan (Department of Agricultural Chemistry, Kyungpook National Universit) ;
  • Joo, Gil-Jae (Institute of Agricultural Science & Technolog) ;
  • Rhee, In-Koo (Department of Agricultural Chemistry, Kyungpook National University)
  • Published : 2004.03.01

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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