O-GlcNAc修饰研究进展  

The review of O-GlcNAc modification

作　　者：刘华东[1] 陈永湘[1] 赵玉芬[1] 李艳梅[1] 

机构地区：[1]清华大学化学系生命有机磷化学及化学生物学教育部重点实验室,北京100084

出　　处：《中国科技论文在线》2007年第8期543-549,共7页

基　　金：高等学校博士学科点专项科研基金(20030003049)

摘　　要：O-GlcNAc糖基化修饰作为一种特殊的蛋白质翻译后修饰形式,动态调节细胞信号传导途径中很多酶的功能,与磷酸修饰有"阴阳调节"关系,正在成为研究的热点。本文综述了近年来O-GlcNAc糖基化修饰酶及其供体底物的研究进展。A hallmark of signal transduction is the dynamic and inducible post-translational modification of proteins. In addition to the well characterized phosphorylation of proteins,many nuclear and cytoplasmic proteins are covalently modified by the linkage of monosaccharide N-acetylglucosamine（GlcNAc） to serine or threonine,a reaction catalyzed by O-GlcNAc transferase（OGT） . More and more evidences have indicated that the O-GlcNAc modification has the yin–yang relationship with phosphorylation. Herein,newly results about enzymes and substrate were reviewed.

关 键 词：化学生物学 O-GlcNAc修饰 UDP-GLCNAC OGT O-GLCNACASE 

分 类 号：Q75[生物学—分子生物学]