![]() Table 1: Differences between N-linked and O-linked glycosylation In contrast, O-linked glycosylation typically includes only a single sugar residue added to a serine or threonine residue. In N-linked glycosylation, a protein can exhibit multiple glycan linkages ranging from one to many. the seemingly insignificant difference in sugar linkage may result in a pronounced difference in the core structure of the sugar, where N-linked sugars adopt the high mannose type core structure, whereas O-linked sugars offer a more extensive range of core structures, including core 1, core 2, and core 3.Īdditionally, another important contrast between N-linked and O-linked glycosylation relates to the type of linkage between the sugar and the protein.įurthermore, the amount of sugar added in N-linked and O-linked glycosylation differs. While N-linked glycosylation connects the sugar to an asparagine (N) residue, O-linked glycosylation prefers a serine or threonine (O) residue instead. The data in Table 1 are a summary and overview of the differences between N-linked and O-linked glycosylation.įirst and foremost, the disparity in the type of amino acid residues to which the sugar is attached serves as a fundamental divergence. This intricate and elaborate process is initiated by the addition of a single sugar residue to the serine or threonine residue of the nascent protein, resulting in a unique and diverse array of glycosylated biomolecules.ĭiagram showing the structure of N-linked and O-linked glycosylation types (Lin et al., 2020) Differences between N-linked and O-linked Glycosylation O-linked glycosylation, which entails the attachment of the glycan to the oxygen atom of the amino acid serine or threonine (O), is a type of glycosylation that occurs primarily in the Golgi apparatus. This complex and multifaceted process, which is initiated by the transfer of a preformed oligosaccharide from a lipid carrier to the nascent protein, is predominantly carried out in the ER and Golgi apparatus. N-linked glycosylation, which involves the glycan being connected to the nitrogen atom of the amino acid asparagine (N), reigns supreme as the most abundant form of glycosylation in eukaryotic cells, accounting for over 90% of all glycosylation events. ![]() ![]() The diverse world of glycosylation is classified into two main categories: N-linked and O-linked glycosylation, each with its own unique molecular complexities and intricacies. In eukaryotic cells, glycosylation is among the most prevalent post-translational modifications, playing a pivotal role in protein folding, stability, and cell signaling. This critical process takes place in two distinct subcellular organelles: the endoplasmic reticulum (ER) and the Golgi apparatus. The complex and intricate process of glycosylation involves the addition of carbohydrate molecules, also known as glycans, to an array of biomolecules, including proteins and lipids. ![]()
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