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

被引：48
|
作者：
Bao, YP
Jemth, P
Mannervik, B
Williamson, G
机构：
[1] FOOD RES INST,DEPT BIOCHEM,NORWICH LAB,NORWICH NR4 7UA,NORFOLK,ENGLAND
[2] UNIV UPPSALA,CTR BIOMED,DEPT BIOCHEM,S-75123 UPPSALA,SWEDEN
来源：
FEBS LETTERS | 1997年 / 410卷 / 2-3期
基金：
英国生物技术与生命科学研究理事会;
关键词：
phospholipid hydroperoxide glutathione peroxidase; thymine hydroperoxide; glutathione transferase; glutathione peroxidase; selenium;
D O I：
10.1016/S0014-5793(97)00591-7
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码：210 / 212
页数：3
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