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Full-Text Articles in Physical Sciences and Mathematics
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 …
Progress Towards The Substrate-Bound Structure Of Streptococcus Pneumoniae Sortase A, Nicholas M. Horvath
Progress Towards The Substrate-Bound Structure Of Streptococcus Pneumoniae Sortase A, Nicholas M. Horvath
WWU Graduate School Collection
Sortases are cysteine transpeptidases found primarily on the cell surface of Gram-positive bacteria. Sortase-mediated ligations have become an attractive option for protein modification chemistry, enabling the synthesis of a wide range of non-natural polypeptide derivatives. Attempts at understanding how these enzymes recognize and bind substrates are integral to furthering their usefulness in protein engineering and, potentially, treatment of bacterial diseases. However, the variable substrate specificity and activity between homologs of these enzymes is not yet fully understood. Of specific interest to us is sortase A from Streptococcus pneumoniae (SrtApneu), as it demonstrates a broad substrate tolerance not …