ArticleThe Journal of biological chemistry2014
Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from Porphyromonas gingivalis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Arginine metabolism as a mutualistic strategy in the interaction between Porphyromonas gingivalis and Filifactor alocis.Nature communications · 2026Article
- A DPP inhibitor suppresses periodontitis via antibacterial effect targeting Porphyromonas gingivalis.Scientific reports · 2026Article
- Periodontitis and GLP-1 pathways: a new frontier in oral-systemic health connections -a scoping review.Frontiers in clinical diabetes and healthcare · 2025Review
- Dipeptidyl-Peptidase-4 and Glucagon-like-Peptide-1, a Link in the Connection between Periodontitis and Diabetes Mellitus-What Do We Know So Far?-A Scoping Review.Journal of clinical medicine · 2024Article
- Curcumin inhibits growth ofJournal of oral microbiology · 2024Article
- Immunoelectron Microscopic Analysis of Dipeptidyl-Peptidases and Dipeptide Transporter Involved in Nutrient Acquisition in Porphyromonas gingivalis.Current microbiology · 2023Article
- Novel hit of DPP-4Is as promising antihyperglycemic agents with dual antioxidant/anti-inflammatory effects for type 2 diabetes with/without COVID-19.Bioorganic chemistry · 2022Article
- Salivary metabolites associated with a 5-year tooth loss identified in a population-based setting.BMC medicine · 2021Article
- Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7.Scientific reports · 2021Article
- Dipeptidyl-peptidases: Key enzymes producing entry forms of extracellular proteins in asaccharolytic periodontopathic bacterium Porphyromonas gingivalis.Molecular oral microbiology · 2021Review
- Metabolic cooperativity betweenJournal of oral microbiology · 2020Article
- Fragment-based discovery of the first nonpeptidyl inhibitor of an S46 family peptidase.Scientific reports · 2019Article
- Dominant prevalence ofJournal of dental sciences · 2017Article
- Degradation of Incretins and Modulation of Blood Glucose Levels by Periodontopathic Bacterial Dipeptidyl Peptidase 4.Infection and immunity · 2017Article
- Bacterial protease uses distinct thermodynamic signatures for substrate recognition.Scientific reports · 2017Article
- A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain.PloS one · 2017Article
- A Porphyromonas gingivalis Periplasmic Novel Exopeptidase, Acylpeptidyl Oligopeptidase, Releases N-Acylated Di- and Tripeptides from Oligopeptides.The Journal of biological chemistry · 2016Article
- Exopeptidases and gingipains inThe Japanese dental science review · 2016Review
- Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.Scientific reports · 2015Article
- Comparative genome analysis and identification of competitive and cooperative interactions in a polymicrobial disease.The ISME journal · 2015Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN_0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 μM and 11.02 μM(-1) s(-1), respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.
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