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Isopeptide Ligations Catalyzed By Streptococcus Suis Sortase A, Sarah Bowersox
Isopeptide Ligations Catalyzed By Streptococcus Suis Sortase A, Sarah Bowersox
WWU Graduate School Collection
Chemically modified proteins are critical components of modern therapeutics and basic research. To generate non-natural protein derivatives, bacterial sortase enzymes have been effective due to their ability to catalyze selective ligations between protein targets and functional groups that are uncommon in nature. Thus far, the enzymatic approach using sortase has been limited to modifications at the termini of peptide chains. Here we describe efforts to develop a sortase-mediated strategy for the formation of isopeptide bonds at the side chains of internal lysine residues. To this end, we have identified a sortase A homolog from Streptococcus suis (SrtAsuis) that …