Chlorothalonil-biotransformation by glutathione S-transferase of Escherichia coli. 2004

Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
Institute of Agricultural Science & Technology , Kyungpook National University, Daegu 702-701, Korea.

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.

UI MeSH Term Description Entries
D009570 Nitriles Organic compounds containing the -CN radical. The concept is distinguished from CYANIDES, which denotes inorganic salts of HYDROGEN CYANIDE. Nitrile
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005978 Glutathione A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides. Reduced Glutathione,gamma-L-Glu-L-Cys-Gly,gamma-L-Glutamyl-L-Cysteinylglycine,Glutathione, Reduced,gamma L Glu L Cys Gly,gamma L Glutamyl L Cysteinylglycine
D005982 Glutathione Transferase A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite. Glutathione S-Alkyltransferase,Glutathione S-Aryltransferase,Glutathione S-Epoxidetransferase,Ligandins,S-Hydroxyalkyl Glutathione Lyase,Glutathione Organic Nitrate Ester Reductase,Glutathione S-Transferase,Glutathione S-Transferase 3,Glutathione S-Transferase A,Glutathione S-Transferase B,Glutathione S-Transferase C,Glutathione S-Transferase III,Glutathione S-Transferase P,Glutathione Transferase E,Glutathione Transferase mu,Glutathione Transferases,Heme Transfer Protein,Ligandin,Yb-Glutathione-S-Transferase,Glutathione Lyase, S-Hydroxyalkyl,Glutathione S Alkyltransferase,Glutathione S Aryltransferase,Glutathione S Epoxidetransferase,Glutathione S Transferase,Glutathione S Transferase 3,Glutathione S Transferase A,Glutathione S Transferase B,Glutathione S Transferase C,Glutathione S Transferase III,Glutathione S Transferase P,Lyase, S-Hydroxyalkyl Glutathione,P, Glutathione S-Transferase,Protein, Heme Transfer,S Hydroxyalkyl Glutathione Lyase,S-Alkyltransferase, Glutathione,S-Aryltransferase, Glutathione,S-Epoxidetransferase, Glutathione,S-Transferase 3, Glutathione,S-Transferase A, Glutathione,S-Transferase B, Glutathione,S-Transferase C, Glutathione,S-Transferase III, Glutathione,S-Transferase P, Glutathione,S-Transferase, Glutathione,Transfer Protein, Heme,Transferase E, Glutathione,Transferase mu, Glutathione,Transferase, Glutathione,Transferases, Glutathione
D001711 Biotransformation The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.

Related Publications

Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
August 2004, Biochemical and biophysical research communications,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
December 1994, Toxicon : official journal of the International Society on Toxinology,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
September 1989, Archives of biochemistry and biophysics,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
November 1989, Journal of bacteriology,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
September 2006, The Journal of pharmacology and experimental therapeutics,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
November 2000, Microbiology (Reading, England),
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
May 1990, Archives of biochemistry and biophysics,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
March 2014, Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
October 2000, The Science of the total environment,
Young-Mog Kim, and Kunbawui Park, and Soon-Hyun Jung, and Jun-Ho Choi, and Won-Chan Kim, and Gil-Jae Joo, and In-Koo Rhee
March 1992, Gene,
Copied contents to your clipboard!