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Which amino acid is glycosylated?

Published in Protein Glycosylation 2 mins read

Glycosylation, a crucial post-translational modification that plays vital roles in many biological processes, can occur on several amino acids. The amino acids that may be glycosylated include asparagine, arginine, cysteine, glutamine, hydroxylysine, hydroxyproline, serine, threonine, tryptophan, and tyrosine.

Understanding Protein Glycosylation

Protein glycosylation is a complex enzymatic process where carbohydrate chains (glycans) are attached to proteins. This modification significantly impacts a protein's structure, stability, folding, and function, influencing everything from cell recognition and signaling to immune responses. There are various types of glycosylation, with the most common being N-linked and O-linked glycosylation, depending on the atom to which the glycan is attached.

Key Glycosylated Amino Acids

Of the 20 canonical amino acids, ten of them and their derivatives have been identified as potential sites for glycosylation. These amino acids offer specific residues where the glycan structures can be covalently linked.

The amino acids capable of being glycosylated are:

Amino Acid Name Abbreviation
Asparagine Asn
Arginine Arg
Cysteine Cys
Glutamine Gln
Hydroxylysine HydroxyLys
Hydroxyproline HydroxyPro
Serine Ser
Threonine Thr
Tryptophan Trp
Tyrosine Tyr

Specific Considerations in Animal Cells

While many amino acids can undergo glycosylation, it's important to note that the occurrence can vary depending on the biological system. For instance, among the listed amino acids, the glycosylation of hydroxyproline has generally not been observed in animal cells, even though other amino acids are commonly glycosylated in these organisms.

Significance of Glycosylation

The modification of proteins by glycans is fundamental to numerous biological processes:

  • Protein Folding and Stability: Glycans can assist in proper protein folding and enhance their stability.
  • Cell-Cell Recognition: Glycoproteins on the cell surface are vital for cell communication and recognition processes, such as in the immune system.
  • Signaling: Glycans can act as ligands for receptors, mediating various cellular signaling pathways.
  • Immune Response: Glycosylation plays a critical role in distinguishing self from non-self, influencing antigenicity and immunogenicity.