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

页码：210 / 212

页数：3

共 30 条

[1]

Bao YP, 1996, J LIPID RES, V37, P2351

[2]

Buege J A, 1978, Methods Enzymol, V52, P302

[3] PURIFICATION OF A CYTOSOLIC ENZYME FROM HUMAN LIVER WITH PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE-PEROXIDASE ACTIVITY [J].