Abstract
The discovery of glutathione S-transferases (GSTs; E.C. 2.5.1.18) active in the metabolism of carcinogens dates back to Booth et al. (1961). GSTs were initially believed to serve as intracellular transport proteins for endogenous compounds with limited solubility in water, thereby acting as an intracellular equivalent to albumin. In this assumed capacity of reversible binding and transport of various ligands, the corresponding protein was named ligandin (Litwack et al., 1971). Following the discovery of abundant GST occurrence in most forms of arerobic life including plants, and the GST-catalysed conjugation of a wide variety of electrophilic substrates with glutathione, GSTs are now generally considered to play a crucial role in the detoxification of foreign compounds (for reviews see Mannervik, 1985; Ketterer, 1988; Mannervik and Danielson, 1988; Sies and Ketterer, 1988). GSTs are also believed to provide cellular protection by covalent binding of reactive electrophiles to the enzyme itself resulting in immobilization and inactivation of the compound.
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© 1991 Plenum Press, New York
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Oesch, F., Gath, I., Igarashi, T., Glatt, H., Oesch-Bartlomowicz, B., Thomas, H. (1991). Role of the Well-Known Basic and Recently Discovered Acidic Glutathione S-Transferases in the Control of Genotoxic Metabolites. In: Witmer, C.M., Snyder, R.R., Jollow, D.J., Kalf, G.F., Kocsis, J.J., Sipes, I.G. (eds) Biological Reactive Intermediates IV. Advances in Experimental Medicine and Biology, vol 283. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5877-0_3
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DOI: https://doi.org/10.1007/978-1-4684-5877-0_3
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