N-乙酰氨基葡萄糖转移酶(OGT)研究进展  

A review on N-acetylglucosamine transferase(OGT)

作　　者：孙红[1] 马晓峰[1] 任飞飞[1] 张连文[1] 王鹏[1] 

机构地区：[1]南开大学药学院,天津300071

出　　处：《生命科学》2011年第7期643-647,共5页Chinese Bulletin of Life Sciences

基　　金：国家重点基础研究发展计划("973"计划)(2007CB914403);国家自然科学基金项目(30970644)

摘　　要：O-GlcNAc是一种广泛存在于蛋白质丝/苏氨酸残基上的动态、可逆的蛋白质翻译后修饰,广泛分布在细胞浆和细胞核中,参与调节多种细胞途径。研究表明蛋白质的O-GlcNAc糖基化与神经退行性疾病、糖尿病和癌症等疾病相关。在体内,O-GlcNAc动态修饰由N-乙酰氨基葡萄糖转移酶(OGT)和N-乙酰氨基葡萄糖苷酶(OGA)协同完成。近年来,OGT逐渐成为糖生物学领域的研究热点,在其结构、作用机制及晶体学方面取得了较大进展。N-acetylglucosamine （O-GlcNAc） modification on protein serines/threonines is a dynamic, inducible and abundant post-translational modification, which is found on numerous cytoplasm and nucleus proteins, regulating many cellular processes. It has been demonstrated that O-GlcNAc plays important roles in some human diseases, such as diabetes and neurodegenerative diseases. O-GlcNAcylation is regulated by O-GlcNAc transferase （OGT） and O-GlcNAcase （OGA） in vivo. The past decades has seen a mass of research on OGT, include studies on the protein structure and the mechanism linked to many important diseases. Recently, OGT is becoming the spotlight in glyco-biological research.

关 键 词：O-GlcNAc糖基化 N-乙酰氨基葡萄糖转移酶(OGT) 作用机制 晶体结构 

分 类 号：Q55[生物学—生物化学]