Journal of Microbiology

Kunbawui Park

1 Article

Chlorothalonil-Biotransformation by Glutathione S-Transferase of Escherichia coli: Young-Mog Kim , Kunbawui Park , Soon-Hyun Jung , Jun-Ho Choi , Won-Chan Kim , Gil-Jae Joo , In-Koo Rhee; J. Microbiol. 2004;42(1):42-46.; DOI: https://doi.org/2002 [pii]

Abstract PDF: 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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