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• W2022715098 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." @default.
• W2022715098 created "2016-06-24" @default.
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• W2022715098 date "2011-10-10" @default.
• W2022715098 modified "2023-10-11" @default.
• W2022715098 title "Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9" @default.
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• W2022715098 doi "https://doi.org/10.1016/j.febslet.2011.10.009" @default.
• W2022715098 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22001206" @default.
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