REDUCTION OF THYMINE HYDROPEROXIDE BY PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE-PEROXIDASE AND GLUTATHIONE TRANSFERASES

Citation
Yp. Bao et al., REDUCTION OF THYMINE HYDROPEROXIDE BY PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE-PEROXIDASE AND GLUTATHIONE TRANSFERASES, FEBS letters, 410(2-3), 1997, pp. 210-212
Citations number
30
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
410
Issue
2-3
Year of publication
1997
Pages
210 - 212
Database
ISI
SICI code
0014-5793(1997)410:2-3<210:ROTHBP>2.0.ZU;2-O
Abstract
Thymine hydroperoxide (5-hydroperoxymethyluracil), a model compound re presenting products of oxidative damage to DNA, is a substrate for glu tathione peroxidase and some isoforms of glutathione transferase. In t his paper, we show that selenium-dependent human phospholipid hydroper oxide 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 va rious representatives of glutathione transferases. The results indicat e that Se-PHGPx may be an important enzyme in repairing oxidatively da maged DNA. (C) 1997 Federation of European Biochemical Societies.