Dipeptidyl Peptidase 8 Has Post-Proline Dipeptidyl Aminopeptidase and Prolyl Endopeptidase Activities

  • Joohong Park
  • Katerina Ajami
  • Denise M. T. Yu
  • Mark D. Gorrell
Part of the Advances in Experimental Medicine and Biology book series (volume 575)

5. Conclusions

We report an expression and purification procedure to produce homogeneous, active human DP8 and DPIV. The most interesting discovery was that DP8 specifically has both prolyl dipeptidyl aminopeptidase and PEP activities. DPIV inhibitors varied in their selectivity against DP8 but all DP8 activities were inhibited by the irreversible DPIV inhibitor ValboroPro. These data indicate that DP8 is a multifunctional enzyme and that therapeutics based on DPIV inhibition should be counter-screened against DP8.


Celiac Disease Cell Culture Supernatant Dipeptidyl Peptidase Prolyl Endopeptidase Prolyl Oligopeptidase 
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Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  • Joohong Park
    • 1
  • Katerina Ajami
    • 1
  • Denise M. T. Yu
    • 1
  • Mark D. Gorrell
    • 1
  1. 1.A. W. Morrow Gastroenterology and Liver Centre at Royal Prince Alfred Hospital, Centenary Institute of Cancer Medicine and Cell Biology and The Discipline of MedicineUniversity of SydneySydneyAustralia

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