@article{oai:nagasaki-u.repo.nii.ac.jp:00002737,
 author = {Nemoto, Takayuki K. and Ono, Toshio and Ohara-Nemoto, Yuko},
 journal = {Analytical Biochemistry},
 month = {May},
 note = {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) (41.40?±?0.83?μM?1?s?1) was highest compared to Met-Leu-, Leu-Leu-, and Phe-Leu-MCA (1.06?3.77?μM?1?s?1). 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., Analytical Biochemistry, 548, pp.78-81; 2018},
 pages = {78--81},
 title = {Establishment of potent and specific synthetic substrate for dipeptidyl-peptidase 7},
 volume = {548},
 year = {2018}
}