Abstract
Booth et al. (1961) were the first to report an enzyme that catalyzed the conjugation of l,2-dichloro-4-nitrobenzene (DCNB) with glutathione in a cytosolic extract of rat liver. Since then, this group of enzymes, glutathione S-transferases (GSTs, EC 2.5.1.18), has been widely observed in many aerobic organisms. The roles of GSTs, and their biochemical and physiological characteristics have been well investigated, most intensively in mammals. Molecular biology studies since the mid-1970s have resulted in significant understanding of the structure of GST genes and regulation of their expression. The three-dimensional structures of GST proteins, established since the early 1990s, have helped further elucidate the evolution and function of these enzymes in biological systems.
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Sun, CN., Huang, SY., Hu, NT., Chung, WY. (2001). Glutathione S-Transferases and Insect Resistance to Insecticides. In: Ishaaya, I. (eds) Biochemical Sites of Insecticide Action and Resistance. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59549-3_11
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DOI: https://doi.org/10.1007/978-3-642-59549-3_11
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