从蛋白质糖基化的结构到功能:以丝氨酸/苏氨酸O-(N-乙酰)葡糖胺修饰为例

The structure and function of protein glycosylation: Example as O-linked β-N-acetylglucosamine(O-GlcNAc) on serine/threonine residues

糖基化作为一种重要的翻译后修饰广泛存在于蛋白质上,对蛋白质的结构和功能具有重要的调控作用。这些糖基化可以发生在各种氨基酸侧链上,且具有很高的结构多样性。然而,在生命科学与化学生物学相关学科的本科生教学中,蛋白质的糖基化修饰却常常被忽略。基于对丝氨酸/苏氨酸O-(N-乙酰)葡糖胺修饰愈发深入的了解,本文将从该修饰的发生、特性和生物学功能等方面进行阐述,通过与磷酸化修饰这一普遍存在的修饰模式的比较,阐明其对于教学和科研的重要性。

As an important type of post translational modification, glycosylation modifications widely exist on proteins, which can play significant roles in regulating the structures and functions of protein substrates. Different types of glycosylation can occur on various kinds of amino acid side chains with highly diverse structures. However, the introduction and application of this kind of modifications is usually omitted in the fundamental education for undergraduates with biochemistry and chemical biology related majors. Based on a gradually deepened understanding of O-linked 13-N-acetyglucosamine modification （O-GlcNAc）, this man- uscript will discuss the catalytic mechanistic study, characterization, and biological functions of it. By com- paring with phosphorylation as a most commonly existing modification, the authors analyze the importance of instructing this modification mode for undergraduate course study and scientific research.