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.
