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. Author manuscript; available in PMC: 2018 Jul 19.
Published in final edited form as: Bioconjug Chem. 2017 Jun 22;28(7):1867–1877. doi: 10.1021/acs.bioconjchem.7b00175

Figure 2.

Figure 2

Mechanism of sortase-mediated ligations. The ligation requires a substrate to bear a LPXTG peptide tag. This peptide tag is recognized by sortase A. The enzyme cleaves between threonine and glycine residues to form an acylenzyme intermediate. The acyl-enzyme intermediate is then susceptible to nucleophilic attack by a ligand bearing an N-terminal glycine residue, leading to the formation of an amide bond between the substrate and the ligand.