Journal Article Establishment of potent and specific synthetic substrate for dipeptidyl-peptidase 7

Nemoto, Takayuki K.  ,  Ono, Toshio  ,  Ohara-Nemoto, Yuko

548pp.78 - 81 , 2018-05-01 , Elsevier Inc.
ISSN:00032697
Description
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.
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http://naosite.lb.nagasaki-u.ac.jp/dspace/bitstream/10069/37985/1/AnalBiochem548_78.pdf

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