Chlorothalonil-biotransformation by glutathione S-transferase of Escherichia coli.
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.
Kim
Young-Mog
YM
Institute of Agricultural Science & Technology , Kyungpook National University, Daegu 702-701, Korea.
Park
Kunbawui
K
Jung
Soon-Hyun
SH
Choi
Jun-Ho
JH
Kim
Won-Chan
WC
Joo
Gil-Jae
GJ
Rhee
In-Koo
IK
D001711:Biotransformation; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D005982:Glutathione Transferase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D009570:Nitriles / Q000378:metabolism*; D010957:Plasmids; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D009570:Nitriles; D011994:Recombinant Proteins; D005982:Glutathione Transferase; D005978:Glutathione; C005806:tetrachloroisophthalonitrile