Peptide Sulfation

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  • Published date: July 18, 2019
    • Shirley, New York, United States

Peptide Sulfation is a common post-translational modification of tyrosine residues in eukaryotes that is known to have a widespread occurrence among proteins of multicellular eukaryotic organisms. Studies on tyrosine-sulfated proteins have shown a major role in enhancing protein-protein interactions, and it is found to be implicated in multiple biological processes. Due to sulfation plays a role in strengthening protein-protein interactions, so types of human proteins known to undergo tyrosine sulfation include G-protein-coupled receptors, adhesion molecules, serine protease inhibitors, coagulation factors, hormones and extracellular matrix proteins. Meanwhile, tyrosine O-sulfate is a stable molecule and is excreted in urine in animals. In addition, studies have shown that it may be observed that tyrosine sulfation has effects on the growth of the mice, such as fecundity, body weight and postnatal viability by knock-out of TPST (tyrosylprotein sulfotransferase) genes in mice.

Cathy Miller
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