| Title : Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9 - Tang_2011_FEBS.Lett_585_3409 |
| Author(s) : Tang HK , Chen KC , Liou GG , Cheng SC , Chien CH , Tang HY , Huang LH , Chang HP , Chou CY , Chen X |
| Ref : FEBS Letters , 585 :3409 , 2011 |
|
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. |
| PubMedSearch : Tang_2011_FEBS.Lett_585_3409 |
| PubMedID: 22001206 |
| Gene_locus related to this paper: human-DPP4 , human-DPP9 |
| Gene_locus | human-DPP4 human-DPP9 |
Tang HK, Chen KC, Liou GG, Cheng SC, Chien CH, Tang HY, Huang LH, Chang HP, Chou CY, Chen X (2011)
Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9
FEBS Letters
585 :3409
Tang HK, Chen KC, Liou GG, Cheng SC, Chien CH, Tang HY, Huang LH, Chang HP, Chou CY, Chen X (2011)
FEBS Letters
585 :3409