Study on the biochemical characterization of herbicide detoxification enzyme, glutathione S-transferase.
To gain further insight into herbicide detoxification, we studied the herbicide activity and specificity toward glutathione S-transferases from human and rice. In this study, the genes of the plant specific phi and tau class GST enzymes from Oryza sativa (OsGST) and human pi class GST enzyme (hGSTP1-1) were cloned and expressed in Escherichia coli with the pET and pKK vector systems, respectively. The gene products were purified to homogeneity by GSH Sepharose affinity column chromatography. The herbicide specificity of the enzymes was investigated by enzyme-catalyzed conjugation of GSH with chloroacetanilide, diphenylether and chloro-s-triazine herbicides. The hGSTP1-1 showed very high specific activity toward atrazine. On the other hand, the phi class OsGST enzymes showed high specific activity toward chloroacetanilide herbicides, acetochlor, alachlor and metolachlor. The tau class GST enzymes displayed remarkable activity toward the diphenylether herbicide, fluorodifen. From these results, we conclude that the phi and the tau class GST enzymes show herbicide specificities and also they play an important role in the detoxification reaction of plant toward herbicides.
Cho
Hyun-Young
HY
Department of Chemistry, College of Natural Sciences, Chung-Ang University, Seoul, Republic of Korea.
Kong
Kwang-Hoon
KH
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology; D005982:Glutathione Transferase / Q000378:metabolism*; D006540:Herbicides / Q000378:metabolism*; D006801:Humans; D012275:Oryza / Q000201:enzymology; D013379:Substrate Specificity
D006540:Herbicides; D005982:Glutathione Transferase