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tyrosylprotein sulfotransferase
Tyrosylprotein sulfotransferase is an enzyme that catalyzes tyrosine sulfation.
== Function ==
Tyrosylprotein Sulfotransferase is the enzyme that catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. It utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and binds proteins with target tyrosine residues to eventually form the tyrosine O-sulfate ester group and the desulfonated 3’-phosphoadenosine-5’-phosphate (PAP).
TPST and tyrosine sulfation is involved in a large number of biological and physiological processes. Tyrosine sulfation has been found to be an important part of the inflammatory process, leukocyte movement and cytosis, viral cell entrance, and other cell-cell and protein-protein interactions.〔〔 Selection for specific tyrosine residues requires a generally accessible tyrosine residue, and acidic residues within +5 or -5 residues of the target tyrosine.〔〔〔 P-selectin glycoprotein ligand-1 (PSGL-1) has been extensively studied as a substrate for TPST and the importance of sulfation in PSGL-1 and its ability to bind its receptor. Another substrate for TPST, CC-chemokine Receptor 5 (CCR5), has generated interest because of its role as the target protein for the viral entrance of HIV into cells. The importance of CCR5’s sulfation for HIV invasion has led to research on TPST and CCR5, including a characterization of the pattern of sulfation of CCR5.〔 Beyond these two proteins, other notable protein substrates include Cholecystokinin (CCK), Factor V and Factor VIII, gastrin, the leech enzyme hirudin, fibrinogen, Complement component 4, follicle-stimulating hormone receptor (FSHR), and other chemokine and G-protein coupled receptors.〔〔 A full, up-to-date list can be found at (UniProtKB ).
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