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Dipeptidyl peptidases (DPPs) that liberate dipeptides from the N-terminal end of oligopeptides are crucial for the growth of  Porphyromonas  species, anaerobic asaccharolytic gram negative rods that utilize amino acids as energy sources.  Porphyromonas endodontalis  is a causative agent of periapical lesions with acute symptoms and Asp/Glu-specific DPP11 has been solely characterized in this organism. In this study, we identified and characterized two  P. endodontalis  DPPs, DPP5 and DPP7. Cell-associated DPP activity toward Lys-Ala-4-methylcoumaryl-7-amide (MCA) was prominent in  P. endodontalis  ATCC 35406 as compared with the  Porphyromonas gingivalis  strains ATCC 33277, 16-1, HW24D1, ATCC 49417, W83, W50, and HNA99. The level of hydrolysis of Leu-Asp-MCA by DPP11, Gly-Pro-MCA by DPP4, and Met-Leu-MCA was also higher than in the  P. gingivalis  strains. MER236725 and MER278904 are  P. endodontalis  proteins belong to the S9- and S46-family peptidases, respectively. Recombinant MER236725 exhibited enzymatic properties including substrate specificity, and salt- and pH-dependence similar to  P. gingivalis  DPP5 belonging to the S9 family. However, the  k   cat / K   m  figure (194 µM −1 ·sec −1 ) for the most potent substrate (Lys-Ala-MCA) was 18.4-fold higher as compared to the  P. gingivalis  entity (10.5 µM −1 ·sec −1 ). In addition,  P. endodontalis  DPP5 mRNA and protein contents were increased several fold as compared with those in  P. gingivalis . Recombinant MER278904 preferentially hydrolyzed Met-Leu-MCA and exhibited a substrate specificity similar to  P. gingivalis  DPP7 belonging to the S46 family. In accord with the deduced molecular mass of 818 amino acids, a 105-kDa band was immunologically detected, indicating that  P. endodontalis  DPP7 is an exceptionally large molecule in the DPP7/DPP11/S46 peptidase family. The enhancement of four DPP activities was conclusively demonstrated in  P. endodontalis , and remarkable Lys-Ala-MCA-hydrolysis was achieved by qualitative and quantitative potentiation of the DPP5 molecule.

Identification of Dipeptidyl-Peptidase (DPP)5 and DPP7 in Porphyromonas endodontalis, Distinct from Those in Porphyromonas gingivalis