ArticleScientific reports2016
Substrate complexes of human dipeptidyl peptidase III reveal the mechanism of enzyme inhibition.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- Influence of adrenomedullin on the enzymatic activity of dipeptidyl peptidase 3Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Bidirectional crosstalk between the catalytic and moonlighting functions of human dipeptidyl peptidase 3: potential physiological implications.RSC advances · 2026Article
- Lysine Targeting Group-Transfer Chimeras for Proximity Induction.Angewandte Chemie (International ed. in English) · 2026Article
- New Amidino-Substituted Benzimidazole Derivatives as Human Dipeptidyl Peptidase III Inhibitors: Synthesis, In Vitro Evaluation, QSAR, and Molecular Docking Studies.International journal of molecular sciences · 2025Article
- Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III.International journal of molecular sciences · 2023Article
- Influence of Mutations of Conserved Arginines on Neuropeptide Binding in the DPP III Active Site.Molecules (Basel, Switzerland) · 2023Article
- Structural and Functional Characterization of a New Bacterial Dipeptidyl Peptidase III Involved in Fruiting Body Formation in Myxobacteria.International journal of molecular sciences · 2022Article
- Health Beneficial Bioactivities of Faba Bean Gastrointestinal (In Vitro) Digestate in Comparison to Soybean and Pea.International journal of molecular sciences · 2022Article
- Dipeptidyl Peptidase 3 Activity as a Promising Biomarker of Bone Fragility in Postmenopausal Women.Molecules (Basel, Switzerland) · 2022Article
- Survey of Dipeptidyl Peptidase III Inhibitors: From Small Molecules of Microbial or Synthetic Origin to Aprotinin.Molecules (Basel, Switzerland) · 2022Review
- Demystifying DPP III Catalyzed Peptide Hydrolysis-Computational Study of the Complete Catalytic Cycle of Human DPP III Catalyzed Tynorphin Hydrolysis.International journal of molecular sciences · 2022Article
- DPP3: From biomarker to therapeutic target of cardiovascular diseases.Frontiers in cardiovascular medicine · 2022Review
- Molecular Dynamics Simulations Study of the Interactions between Human Dipeptidyl-Peptidase III and Two Substrates.Molecules (Basel, Switzerland) · 2021Article
- Efficient Entropy-Driven Inhibition of Dipeptidyl Peptidase III by Hydroxyethylene Transition-State Peptidomimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Triarylborane Dyes as a Novel Non-Covalent and Non-Inhibitive Fluorimetric Markers for DPP III Enzyme.Molecules (Basel, Switzerland) · 2021Article
- Coumarin Derivatives Act as Novel Inhibitors of Human Dipeptidyl Peptidase III: Combined In Vitro and In Silico Study.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Dipeptidyl peptidase 3 modulates the renin-angiotensin system in mice.The Journal of biological chemistry · 2020Article
- Conservation of the conformational dynamics and ligand binding within M49 enzyme family.RSC advances · 2018Article
- The Development of Translational Biomarkers as a Tool for Improving the Understanding, Diagnosis and Treatment of Chronic Neuropathic Pain.Molecular neurobiology · 2018Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human dipeptidyl-peptidase III (hDPP III) is a zinc-dependent hydrolase cleaving dipeptides off the N-termini of various bioactive peptides. Thus, the enzyme is likely involved in a number of physiological processes such as nociception and is also implicated in several forms of cancer. We present high-resolution crystal structures of hDPP III in complex with opioid peptides (Met-and Leu-enkephalin, endomorphin-2) as well as with angiotensin-II and the peptide inhibitor IVYPW. These structures confirm the previously reported large conformational change of the enzyme upon ligand binding and show that the structure of the closed conformation is independent of the nature of the bound peptide. The overall peptide-binding mode is also conserved ensuring the correct positioning of the scissile peptide bond with respect to the catalytic zinc ion. The structure of the angiotensin-II complex shows, how longer peptides are accommodated in the binding cleft of hDPP III. Differences in the binding modes allow a distinction between real substrates and inhibitory peptides or "slow" substrates. The latter displace a zinc bound water molecule necessitating the energetically much less favoured anhydride mechanism as opposed to the favoured promoted-water mechanism. The structural data also form the necessary framework for the design of specific hDPP III inhibitors.
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