Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 210-212 |
| Number of pages | 3 |
| Journal | FEBS Letters |
| Volume | 410 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 30 Jun 1997 |
| Externally published | Yes |
Keywords
- Glutathione peroxidase
- Glutathione transferase
- Phospholipid hydroperoxide glutathione peroxidase
- Selenium
- Thymine hydroperoxide