Proteins Post-translational Modifications
Proteins Metabolism

Author: Gianpiero Pescarmona
Date: 24/04/2009


Proteins Post-translational Modifications

Post-translational modification regulates the qualitative and quantitative control of a huge number of proteins in eukaryotes. Multiple sites may be targeted by a wide range of modifications, such as

  • Phosphorylation, the addition of a phosphate group, usually to serine, tyrosine, threonine or histidine
  • Vitamin K dependent Carboxylation
  • proline hydroxylation
  • glycosylation
  • sulphation
  • methylation
  • sumoylation
  • citrullination
  • farnesylation
  • myristoylation
  • biotinylation
  • ubiquitination
  • proteolytic cleavage

These complex processes require a multitude of specific enzymes that are species and tissue specific.
The subsequent changes modulate the physicochemical properties, folding, conformation, distribution, stability, activity and immunogenicity of the protein.
The qualitative and quantitative differences in the post-translational modifications of glycoproteins may have consequences for the bio-distribution, activity and immunogenic potential of the enzyme.

AddThis Social Bookmark Button