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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

All protocols are individualized at APRN intake

No controlled trial has tested the combination, and the strongest ingredient evidence (L-carnitine) shows only about 11.3 kg average difference