glycosylation
A catch-all name for a set of very common and very heterogeneous chemical modifications. Sugar moieties can be attached to the sidechain hydroxyl groups of Ser/Thr or to the sidechain amide groups of Asn.
Glycosylation (glye-KAW-sil-AY-shun) The process of adding specialized chains of sugar molecules to proteins or lipids; occurs in the ER and Golgi.
Core glycosylation The addition of carbohydrates to proteins and the processing of these carbohydrates that takes place in the endoplasmic reticulum.
Glycosylation - the addition of specific short-chain sugars to asparagine, serine, or threonine - is very common in membrane proteins that form structural components of the cell surface.
The major processing activity is glycosylation: the adding of sugar molecules to form glycoproteins.
In some cells, e.g.
Glycosylation. Glycosylation involves the attachment of oligosaccharides.
Disulfide bond formation and rearrangement. Disulfide bonds stabilize the tertiary and quaternary structure of many proteins.
Sarcoplasmic reticulum.
Proteins may be modified in a wide variety of ways, including phosphorylation (addition or a phosphate group), adenylation (addition of an adenine group), glycosylation (addition of a sugar group), acylation (addition of a lipid group), ...
Amadori rearrangement, a rearrangement that occurs in cross-linking reactions seen in collagen and in protein glycosylations; e.g., conversion of n-glycosides of aldoses to N-glycosides of the corresponding ketoses.
A group of genetic defects in sugar metabolism are termed congenital disorders of glycosylation (CDG), which result from abnormal carbohydrate metabolism, specifically the abnormal synthesis of N-linked oligosaccharides.
Post-translational processing: The reactions which alter a protein's covalent structure, such as phosphorylation, glycosylation or proteolytic cleavage.
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 See also: Protein, Trans, Proteins, Organ, Cell
  
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