Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7556963 | Analytical Biochemistry | 2018 | 4 Pages |
Abstract
Bacterial dipeptidyl-peptidase (DPP) 7 liberates a dipeptide with a preference for aliphatic and aromatic penultimate residues from the N-terminus. Although synthetic substrates are useful for activity measurements, those currently used are problematic, because they are more efficiently degraded by DPP5. We here aimed to develop a potent and specific substrate and found that the kcat/Km value for Phe-Met-methylcoumaryl-7-amide (MCA) (41.40â¯Â±â¯0.83â¯Î¼Mâ1â¯sâ1) was highest compared to Met-Leu-, Leu-Leu-, and Phe-Leu-MCA (1.06-3.77â¯Î¼Mâ1â¯sâ1). Its hydrolyzing activity was abrogated in a Porphyromonas gingivalis dpp7-knockout strain. Conclusively, we propose Phe-Met-MCA as an ideal synthetic substrate for DPP7.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Takayuki K. Nemoto, Toshio Ono, Yuko Ohara-Nemoto,