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Comparing the structures of the prokaryotic X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis and eukaryotic DPP4 demonstrates that the residues most implicated in X-PDAP activity are conserved in the same positions and orientations of DPP4, despite very different domains flanking the catalytic domain, different dimer organization, and substrate selectivity processes

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