4-Hydroxyalk-2-enals are substrates for glutathione transferase.
The 4-hydroxyalk-2-enals are established products of lipid peroxidation that are conjugated with intracellular glutathione. Cytosolic glutathione transferases from rat liver were shown to give high specific activities with 4-hydroxynonenal and 4-hydroxydecenal. The isoenzyme giving the highest specific activity was glutathione transferase 4-4. The rate of the spontaneous conjugation reaction is negligible in comparison with the rate calculated for the cellular concentration of the glutathione transferases. It is proposed that a major biological function of the glutathione transferases is to protect the cell against products of oxidative metabolism, such as epoxides, organic hydroperoxides, and 4-hydroxyalkenals.
D000447:Aldehydes / Q000378:metabolism*; D000818:Animals; D004137:Dinitrochlorobenzene / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D051381:Rats; D013379:Substrate Specificity
D000447:Aldehydes; D004137:Dinitrochlorobenzene; D007527:Isoenzymes; C044135:4-hydroxy-2-decenal; D005982:Glutathione Transferase; C027576:4-hydroxy-2-nonenal