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 language | English |
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Pages (from-to) | 3409-3414 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 585 |
Issue number | 21 |
DOIs | |
State | Published - Nov 4 2011 |
Externally published | Yes |
Keywords
- Analytical ultracentrifugation
- Dimerization
- Dipeptidyl peptidase 9
- Dipeptidyl peptidase-IV
- Propeller loop