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. Author manuscript; available in PMC: 2021 Apr 23.
Published in final edited form as: Mol Pharm. 2017 May 8;14(6):1906–1915. doi: 10.1021/acs.molpharmaceut.7b00009

Figure 6.

Figure 6.

Schematic of cleavage positions for proline-specific peptidases. This shows the general cleavage sites for proline-specific peptidases on a peptide with a free N-terminus. DPPs have the highest cleavage efficiency when removing dipeptides from sequences as shown; however, they can also cleave tri- and tetrapeptides on the carboxyl side of proline residues at a reduced efficiency. PIP prefers to cleave a single proline residue off sequences but can cleave di- and tripeptides on the carboxyl side of prolines at reduced efficiency as well. APP is responsible for the removal of a single residue on the amino side of proline. APP: aminopeptidase P, DPP: dipeptidyl peptidase, PE: prolyl endopeptidase, PIP: proline iminopeptidase.