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  2. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...

  3. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    N-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell–extracellular matrix attachment. The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria.

  4. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    N-Linked glycosylation involves oligosaccharide attachment to asparagine via a beta linkage to the amine nitrogen of the side chain. [7] The process of N-linked glycosylation occurs cotranslationally, or concurrently while the proteins are being translated. Since it is added cotranslationally, it is believed that N-linked glycosylation helps ...

  5. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins. [1] Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification.

  6. Glycation - Wikipedia

    en.wikipedia.org/wiki/Glycation

    In contrast with glycation, glycosylation is the enzyme-mediated ATP-dependent attachment of sugars to a protein or lipid. [1] Glycosylation occurs at defined sites on the target molecule. It is a common form of post-translational modification of proteins and is required for the functioning of the mature protein.

  7. Cerebroside - Wikipedia

    en.wikipedia.org/wiki/Cerebroside

    The glycosyl-transferase catalyzed reaction results in an inversion of the glycosidic bond stereochemistry, changing from α →β. Synthesis of galactosylceramide, and glucosylceramide occurs on the lumenal surface of the endoplasmic reticulum, and on the cytosolic side of the early Golgi membranes respectively.

  8. Dolichol - Wikipedia

    en.wikipedia.org/wiki/Dolichol

    Dolichols play a role in the post-translational modification of proteins known as N-glycosylation in the form of dolichol phosphate.Dolichols function as a membrane anchor for the formation of the oligosaccharide Glc 3 –Man 9 –GlcNAc 2 (where Glc is glucose, Man is mannose, and GlcNAc is N-acetylglucosamine).

  9. Congenital disorder of glycosylation - Wikipedia

    en.wikipedia.org/wiki/Congenital_disorder_of...

    A congenital disorder of glycosylation (previously called carbohydrate-deficient glycoprotein syndrome) is one of several rare inborn errors of metabolism in which glycosylation of a variety of tissue proteins and/or lipids is deficient or defective. Congenital disorders of glycosylation are sometimes known as CDG syndromes.