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A Porphyromonas gingivalis Periplasmic Novel Exopeptidase, Acylpeptidyl Oligopeptidase, Releases N-Acylated Di- and Tripeptides from Oligopeptides


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Title: A Porphyromonas gingivalis Periplasmic Novel Exopeptidase, Acylpeptidyl Oligopeptidase, Releases N-Acylated Di- and Tripeptides from Oligopeptides
Authors: Nemoto, Takayuki K / Ohara-Nemoto, Yuko / Bezerra, Gustavo Arruda / Shimoyama, Yu / Kimura, Shigenobu
Issue Date: 11-Mar-2016
Publisher: American Society for Biochemistry and Molecular Biology Inc.
Citation: Journal of Biological Chemistry, 291(11), pp.5913-5925; 2016
Abstract: Exopeptidases including dipeptidyl- and tripeptidyl-peptidase are crucial for the growth of Porphyromonas gingivalis, a periodontopathic asaccharolytic bacterium that incorporates amino acids mainly as di- and tri-peptides. In this study, we identified a novel exopeptidase, designated acylpeptidyl oligopeptidase (AOP), composed of 759 amino acid residues with active Ser615 and encoded by PGN_1349 in P. gingivalis ATCC 33277. AOP is currently listed as an unassigned S9-family peptidase or prolyl oligopeptidase. Recombinant AOP did not hydrolyze a Pro-Xaa bond. In addition, though sequence similarities to human and archaea-type acylaminoacyl peptidase sequences were observed, its enzymatic properties were apparently distinct from those, as AOP scarcely released an N-acyl-amino acid as compared to di- and tri-peptides, especially with N-terminal modification. The kcat/Km value against benzyloxycarbonyl-Val-Lys- Met-4-methycoumaryl-7-amide, the most potential substrate, was 123.3 ± 17.3 µM-1sec-1, optimal pH was 7-8.5, and the activity was decreased with increased NaCl concentrations. AOP existed predominantly in the periplasmic fraction as a monomer, while equilibrium between monomers and oligomers was observed with a recombinant molecule, suggesting a tendency of oligomerization mediated by the N-terminal region (Met16-Glu101). The three dimensional modeling revealed the three domain structures: residues Met16-Ala126, which has no similar homologue with known structure, residues Leu127-Met495 (β-propeller domain) and residues Ala496-Phe736 (α/β hydrolase domain), and further indicated the hydrophobic S1 site of AOP in accord with its hydrophobic P1 preference. AOP orthologues are widely distributed in bacteria, archaea, and eukaryotes, suggesting its importance for processing of nutritional and/or bioactive oligopeptides.
Keywords: microbial pathogenesis / periodontal disease / peptidase / aminopeptidase / oligomerization / DPF-6 / oligopeptidase B / acylaminoacyl peptidase
URI: http://hdl.handle.net/10069/36584
ISSN: 1083351X
DOI: 10.1074/jbc.M115.687566
Rights: This research was originally published in Journal of Biological Chemistry. Takayuki K. Nemoto, et al. A Porphyromonas gingivalis Periplasmic Novel Exopeptidase, Acylpeptidyl Oligopeptidase, Releases N-Acylated Di- and Tripeptides from Oligopeptides. Journal of Biological Chemistry. 2016; Vol:291(11) pp.5913-5925 © the American Society for Biochemistry and Molecular Biology.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/36584

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