Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9

Hung Kuan Tang, Ku Chuan Chen, Gan Guang Liou, Shu Chun Cheng, Chia Hui Chien, Hsiang Yun Tang, Li Hao Huang, Hui Ping Chang, Chi Yuan Chou, Xin Chen

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The dipeptidyl peptidase (DPP) family members, including DPP-IV, DPP8, DPP9 and others, cleave the peptide bond after the penultimate proline residue and are drug target rich. The dimerization of DPP-IV is required for its activity. A propeller loop located at the dimer interface is highly conserved within the family. Here we carried out site-directed mutagenesis on the loop of DPPIV and identified several residues important for dimer formation and enzymatic activity. Interestingly, the corresponding residues on DPP9 have a different impact whereby the mutations decrease activity without changing dimerization. Thus the propeller loop seems to play a varying role in different DPPs.

Original languageEnglish
Pages (from-to)3409-3414
Number of pages6
JournalFEBS Letters
Volume585
Issue number21
DOIs
StatePublished - Nov 4 2011
Externally publishedYes

Keywords

  • Analytical ultracentrifugation
  • Dimerization
  • Dipeptidyl peptidase 9
  • Dipeptidyl peptidase-IV
  • Propeller loop

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