1. Post Translational Modification
Zachry Theis
Clarity Argall

2. Overview Post Translational Modification Glycosylation
Tyrosine Sulfonation

3. Glycosylation Description Purpose of Glycosylation Mechanism
Types of Glycosylation

4. Description Post Translational Modification Enzymatic Process
Carbohydrate Attachment
Found frequently in ER and golgi

5. Purpose Structural Components Specific Recognition Protein Folding
Endogeneous Recogoniton
Exogeneous Recognition

6. Mechanism
α linkage
β linkage

7. Types of Glycosylation
N-Linked
O-linked
C-Linked
Glycation

8. N-Linked Largely In Eukaryotes Addition to Asparagine
Oligosaccharyltransferase
High Mannose Oligosaccharides
Complex Oligosaccharides

9. O-Linked After N-glycosylation Golgi Serine and Threonine
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase

10. C-Linked
Mannose to Tryptophan
Less common
Thrombospondins

11. Glycation Non Enzymatic Endogeneous or Exogeneous Impairs function
Alzheimer’s and Parkinson

12. Tyrosine Sulfation

13. Tyrosine Sulfation Posttranslational Modification
Sulfate group added to Tyrosine residue of protein
Occurs in Golgi Apparatus
Tyrosine

14. Tyrosylprotein sulfotransferase
Catalyst

15. Mechanism

16. 3'-Phosphoadenosine-5'-phosphosulfate

17. Function Strengthens Protein-Protein Interactions Examples:
Serine Protease Inhibitors
Adhesion Molecules
Coagulation Factors

18. References
Alberts, Bruce. Molecular Biology of the Cell. New York: Garland Science, Print
"Glycosylation." UniProt. UniProt, 20 July Web. 19 Nov <
Varki, Ajit. Essentials of Glycobiology. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, Print