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O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O -glycosylation is a post-translational modification that occurs after the protein has been synthesised.
An example of an O-linked oligosaccharide with β-Galactosyl-(1n3)-α-N-acetylgalactosaminyl-Ser/Thr. Oligosaccharides that participate in O-linked glycosylation are attached to threonine or serine on the hydroxyl group of the side chain. [7]
The two most common linkages in glycoproteins are N-linked and O-linked glycoproteins. [3] An N-linked glycoprotein has glycan bonds to the nitrogen containing an asparagine amino acid within the protein sequence. [4] An O-linked glycoprotein has the sugar is bonded to an oxygen atom of a serine or threonine amino acid in the protein. [4]
O-linked glycans attached to the hydroxyl oxygen of serine, threonine, tyrosine, hydroxylysine, or hydroxyproline side-chains, or to oxygens on lipids such as ceramide. Phosphoglycans linked through the phosphate of a phosphoserine. C-linked glycans, a rare form of glycosylation where a sugar is added to a carbon on a tryptophan side-chain.
The result of glycosyl transfer can be a carbohydrate, glycoside, oligosaccharide, or a polysaccharide. Some glycosyltransferases catalyse transfer to inorganic phosphate or water . Glycosyl transfer can also occur to protein residues, usually to tyrosine , serine , or threonine to give O-linked glycoproteins , or to asparagine to give N-linked ...
Keratan sulfate I (KSI) is N-linked via a high mannose type precursor oligosaccharide. Keratan sulfate II (KSII) and keratan sulfate III (KSIII) are O-linked, with KSII linkages identical to that of mucin core structure, and KSIII linked to a 2-O mannose. Elongation of the keratan sulfate polymer occurs through the glycosyltransferase addition ...
This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. The localization site of this particular enzyme is preponderantly the trans-Golgi. [8]
Sialyltransferases are enzymes that transfer sialic acid to nascent oligosaccharide. [1] Each sialyltransferase is specific for a particular sugar substrate. Sialyltransferases add sialic acid to the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins.