摘要
谷胱甘肽过氧化物酶(glutathione peroxidase,GPx)是在抗氧化防御系统中起到重要作用的一类功能蛋白质,它能够清除多种过氧化物并保护组织细胞免受过氧化损伤。GPx的缺乏会引起多种疾病的发生,因此具有潜在的药用价值。其强大的催化能力主要归功于催化位点中的硒代半胱氨酸(selenocysteine,Sec)。但由于Sec插入到蛋白质中需要一种特殊机制,且这种机制在真核和原核生物中并不相同,很难利用传统基因工程方法在大肠杆菌中制备含硒GPx蛋白。文章对GPx的种类、结构、功能及其表达机制的研究进展进行综述,并总结了几种向蛋白质中引入Sec的方法,以期为开发重组含硒GPx或其替代物提供新思路。
Glutathione peroxidase （GPx） is a member of antioxidant enzyme family and acts as free radical scavengers using glutathione as reducing substrate, which protect tissues and cells from oxidative damage. Lack of GPx activity in human is associated with a variety of diseases. The efficient antioxidant activity depends on the presence of selenocysteine （Sec） at the catalytic site. However, incorporation of Sec into protein occurs in a peculiar way, and the mechanism differs from prokaryotes to eukaryotes. Thus, it is difficult to directly express recombinant selenium-containing GPx in E. coli. This article reviewed classification, structure, function and biosynthetic mechanism of GPx. And then, different methods for production of selenoproteins were summarized.
出处
《生物物理学报》
CAS
CSCD
北大核心
2013年第10期724-737,共14页
Acta Biophysica Sinica
基金
国家自然科学基金项目(30970633
31270851)~~
