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Abstract：
N-linked protein glycosylation is a post-translational modification that exists in all domains of life. It involves two consecutive steps: (i) biosynthesis of a lipid-linked oligosaccharide (LLO), and (ii) glycan transfer from the LLO to asparagine residues in secretory proteins, which is catalyzed by the integral membrane enzyme oligosaccharyltransferase (OST). In the last decade, structural and functional studies of the N-glycosylation machinery have increased our mechanistic understanding of the pathway. The structures of bacterial and eukaryotic glycosyltransferases involved in LLO elongation provided an insight into the mechanism of LLO biosynthesis, whereas structures of OST enzymes revealed the molecular basis of sequon recognition and catalysis. In this review, we will discuss approaches used and insight obtained from these studies with a special emphasis on the design and preparation of substrate analogs.
摘要：
N-连接蛋白糖基化是存在于生命的所有结构域中的翻译后修饰。它涉及两个连续的步骤：（1）生物合成脂质连接的寡糖（LLO），和（2）聚糖从LLO转移到分泌蛋白中的天冬酰胺残基，其由整合膜酶寡糖转移酶(OST)催化。在过去的十年里，N-糖基化机制的结构和功能研究增加了我们对该途径的机制理解。参与LLO延伸的细菌和真核糖基转移酶的结构提供了对LLO生物合成机制的了解。而OST酶的结构揭示了测序识别和催化的分子基础。在这次审查中,我们将讨论使用的方法和从这些研究中获得的见解，特别强调底物类似物的设计和制备。
