Tyrosylprotein sulfotransferase

Seibert C, Cadene M, Sanhz A, Chait BT, Sakmar TP. Tyrosine sulfation of CCR5 N-terminal peptide by tyrosylprotein sulfotransferases 1 and 2 follows a discrete pattern and temporal sequence. Proc Natl Acad Sci U S A 2002 99(17) 11031— 11036. 

Protein sulfation occurs exclusively at tyrosine residues." It has been suggested that up to 1 % of the tyrosine protein content becomes sulfated, which is the most abundant posttranslational modification for tyrosine, with phosphorylation occurring only on 0.5% of tyrosine protein content." Sulfation occurs mostly on excreted proteins or trans-membrane proteins. Sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST), with PAPS as a cosubstrate (Scheme 4). Like kinases, sulfotransferases have a biological inverse known as sulfatases." ... 

Rens-Domiano, S., and Roth, J.A., 1989, Characterization of tyrosylprotein sulfotransferase from rat liver and other tissues. J. Biol. Chem. 264, 899—905... 

Niehrs, C., Kraft, M., Lee, R. W., and Huttner, W. B. (1990). Analysis of the substrate specificity of tyrosylprotein sulfotransferase using synthetic peptides. /. Biol. Chem. 265, 8525-8532. 

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). 

Danan, L. M., Yu, Z., Hoffhines, A. J., Moore, K. L., Leary, J. A. (2008). Mass spectro-metric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2. Journal of the American Society for Mass Spectrometry, 19(10), 1459—1466. 

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. 

Sequential tyrosine sulfation of CXCR4 by tyrosylprotein sulfotransferases. Biochemistry, 47(43), 11251-11262. 

Teramoto, T., Fujikawa, Y., Kawaguchi, Y., Kurogi, K., Soejima, M., Adachi, R., et al. (2013). Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction. Nature Communications, 4, 1572. 

Table 3. List of cloned carbohydrate and tyrosylprotein sulfotransferases. 

R. Beisswanger, D. Corbeil, C. Vannier, C. Thiele, U. Dohrmann, R. Kellner, K. Ashman, C. Niehrs, W. B. Huttner, Existence of distinct tyrosylprotein sulfotransferase genes molecular characterization of tyrosylprotein sulfotransferase-2. Proc. Natl Acad. Scl USA 1998 95, 11134-9. 

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