Journal of Microbiology

  • 제42권1호
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  • Pages.42-46
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  • 2004
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  • 1225-8873(pISSN)
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  • 1976-3794(eISSN)
한국미생물학회 (The Microbiological Society of Korea)
권호 표지

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

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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