Tyrosylprotein sulfotransferase

Tyrosylprotein sulfotransferase is an enzyme that catalyzes tyrosine sulfation.^[1]

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).^[2][3][4]

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.

TPST is a prevalent enzyme, found in many multicellular eukaryotes including mammals, most vertebrates, and a number of invertebrate species as well, including Drosophila melanogaster.^[2][3][10] Its importance can be further demonstrated by the fact as much as 1% of all secreted and membrane tyrosine residues are found to be sulfated.^[6][11]

Mechanism

Within the last two years, using the crystallized structure of the catalytic region of TPST-2 and different experiments other methods using mass spectrometry methods have come to propose two separate mechanisms.

Two-site ping-pong mechanism

A two-site

• Sulfotransferase

References