Reduction of thymine hydroperoxide by phospholipid hydroperoxide glutathione peroxidase and glutathione transferases

FEBS Letters

Jemth, Per¹  Bao, Yongping²  Williamson, Gary²  Mannervik, Bengt¹ 

[1] Department of Biochemistry, Uppsala University, Biochemical Center, Box 576, S-75123 Uppsala, Sweden;Department of Biochemistry, Institute of Food Research, Norwich Laboratory, Norwich Research Park, Colney Lane, Norwich NR4 7UA, UK

关键词: Phospholipid hydroperoxide glutathione peroxidase;    Thymine hydroperoxide;    Glutathione transferase;    Glutathione peroxidase;    Selenium;    Se-PHGPx;    selenium-dependent phospholipid hydroperoxide glutathione peroxidase;    hGST;    human glutathione transferase;    rGST;    rat glutathione transferase;    Thy-OOH;    thymine hydroperoxide;    Se-GPx;    selenium-dependent glutathione peroxidase;    GSH;    glutathione;   

DOI  :  10.1016/S0014-5793(97)00591-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thymine hydroperoxide (5-hydroperoxymethyluracil), a model compound representing products of oxidative damage to DNA, is a substrate for glutathione peroxidase and some isoforms of glutathione transferase. In this paper, we show that selenium-dependent human phospholipid hydroperoxide glutathione peroxidase (Se-PHGPx) exhibits about four orders of magnitude higher activity on thymine hydroperoxide than that of other human enzymes such as selenium-dependent glutathione peroxidase and various representatives of glutathione transferases. The results indicate that Se-PHGPx may be an important enzyme in repairing oxidatively damaged DNA.

【 授权许可】

Unknown