Tyrosylprotein sulfotransferase enzymes

Preparation and Analysis of N-Terminal Chemokine Receptor Sulfopeptides Using Tyrosylprotein Sulfotransferase Enzymes... 

With up to 1% of eukaryotic proteins potentially containing sulfotyrosine residues, sulfation of tyrosines is a common posttranslational modification whose biological impact has only just started to be elucidated (Ludeman Stone, 2014 Moore, 2003 Seibert et al., 2008). In humans and most mammals, there are two isoforms of the enzyme responsible for tyrosine sulfation these enzymes are tyrosylprotein sulfotransferase 1 and 2 (TPST-1 and TPST-2) (Moore, 2003 Seibert Sakmar, 2008). TPST-1 and TPST-2 are located in the irans-Golgi network and this limits tyrosine sulfation to secreted or membrane proteins (Moore, 2003 Seibert Sakmar, 2008). Both enzymes utilize the cosubstrate PAPS, or 3Gphosphoadenosine-5 -phosphosulfate, as the sulfate donor to catalyze the sulfation of a tyrosine s phenolic hydroxyl in a substrate protein or peptide as seen in Fig. 1 (Moore, 2003 Seibert Sakmar, 2008). 

Ouyang, Y., Lane, W. S., Moore, K. L. (1998). Tyrosylprotein sulfotransferase Purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins. Proceedings of the National Academy of Sciences of the United States of America, 95(6), 2896—2901. 

---