ArticleScientific reports2018
Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
- A shark variable new antigen receptor recognizes an occluded epitope of fibroblast activation protein.bioRxiv : the preprint server for biology · 2026Article
- Foldify: Web Application for Protein Structure Prediction.Journal of chemical information and modeling · 2026Article
- Techniques for the determination of dipeptidyl peptidase IV and screening of its inhibitors.Journal of pharmaceutical analysis · 2026Review
- A Structure-activity Relationship (SAR) Insight for the Most Effective Oral Antidiabetic Compounds-A Current Review.Current topics in medicinal chemistry · 2026Review
- Microbial dipeptidyl peptidases of the S9B family as host-microbe isozymes.Science advances · 2025Review
- α/β Hydrolases: Toward Unraveling Entangled Classification.Proteins · 2025Article
- Comparative Binding Study of Gliptins to Bacterial DPP4-like Enzymes for the Treatment of Type 2 Diabetes Mellitus (T2DM).International journal of molecular sciences · 2024Article
- Study on the Mechanism of Interaction between Dipeptidyl Peptidase 4 and Inhibitory Peptides Based on Gaussian Accelerated Molecular Dynamic Simulation.International journal of molecular sciences · 2024Article
- Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.Protein science : a publication of the Protein Society · 2024Article
- 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
- Dipeptidyl peptidase 9 sets a threshold for CARD8 inflammasome formation by sequestering its active C-terminal fragment.Immunity · 2021Article
- Article
- Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review.International journal of molecular sciences · 2019Review
- Commentary: The Potential Role of the Dipeptidyl Peptidase-4-Like Activity From the Gut Microbiota on the Host Health.Frontiers in microbiology · 2018Article
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13 authors.
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Abstract
Dipeptidyl peptidase IV (DPP IV, DPP4, or DAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position. The substrate recognition mechanism has been fully elucidated for mammalian DPP IV by crystal structure analyses but not for bacterial orthologues. Here, we report the crystal structures of a bacterial DPP IV (PmDAP IV) in its free form and in complexes with two kinds of dipeptides as well as with a non-peptidyl inhibitor at 1.90 to 2.47 Å resolution. Acyl-enzyme intermediates were observed for the dipeptide complexes of PmDAP IV, whereas tetrahedral intermediates were reported for the oligopeptide complexes of mammalian DPP IVs. This variation reflects the different structural environments of the active site Arg residues, which are involved in the recognition of a substrate carbonyl group, of mammalian and bacterial enzymes. A phylogenetic analysis revealed that PmDAP IV is a closer relative of dipeptidyl peptidases 8 and 9 (DPP8 and DPP9, DPP IV-family enzymes) than DPP IV. These results provide new insights into the substrate recognition mechanism of bacterial DAP IVs and may assist in the development of selective inhibitors for DAP IVs from pathogenic asaccharolytic bacteria, which utilise proteins or peptides as an energy source.
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