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

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Title: Establishment of potent and specific synthetic substrate for dipeptidyl-peptidase 7
Authors: Nemoto, Takayuki K. / Ono, Toshio / Ohara-Nemoto, Yuko
Issue Date: 1-May-2018
Publisher: Elsevier Inc.
Citation: Analytical Biochemistry, 548, pp.78-81; 2018
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) (41.40 ± 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.
Keywords: Dipeptidyl-peptidase 5 / Dipeptidyl-peptidase 7 / Periodontopathic bacteria / Porphyromonas gingivalis / Substrate specificity
URI: http://hdl.handle.net/10069/37985
ISSN: 00032697
DOI: 10.1016/j.ab.2018.02.008
Rights: © 2018 Elsevier Inc. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/37985

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