Biochemical properties and expression profile of human prolyl dipeptidase DPP9

Hung Kuan Tang, Hsiang Yun Tang, Shu Ching Hsu, Yue Ru Chu, Chia Hui Chien, Chin Hang Shu, Xin Chen

研究成果: 雜誌貢獻期刊論文同行評審

30 引文 斯高帕斯(Scopus)


Dipetidyl peptidase 9 (DPP9) is a prolyl dipeptidase preferentially cleaving the peptide bond after the penultimate proline residue. The biological function of DPP9 is unknown. In this study, we have significantly improved the yield using Strep·Tactin® purification system and characterized the biochemical property of DPP9. Moreover, the dimer interaction mode was investigated by introducing a mutation (F842A) at the dimer interface, which abolished the enzymatic activity without disrupting its quaternary structure. Furthermore, DPP9 was found ubiquitously expressed in fibroblasts, epithelial, and blood cells. Surprisingly, contrary to previous report, we found that the expression levels of DPP8 and DPP9 did not change upon the activation of the PBMC or Jurkat cells. These results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo.

頁(從 - 到)120-127
期刊Archives of Biochemistry and Biophysics
出版狀態已出版 - 15 5月 2009


深入研究「Biochemical properties and expression profile of human prolyl dipeptidase DPP9」主題。共同形成了獨特的指紋。