Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9 |
| |
Authors: | Tang Hung-Kuan Chen Ku-Chuan Liou Gan-Guang Cheng Shu-Chun Chien Chia-Hui Tang Hsiang-Yun Huang Li-Hao Chang Hui-Ping Chou Chi-Yuan Chen Xin |
| |
Institution: | Division of Biotechnology and Pharmaceutical Research, National Health Research Institutes, Miaoli 350, Taiwan, ROC. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|