ArticleScientific reports2014
S46 peptidases are the first exopeptidases to be members of clan PA.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- A DPP inhibitor suppresses periodontitis via antibacterial effect targeting Porphyromonas gingivalis.Scientific reports · 2026Article
- 7-Aminocoumarin-4-acetic Acid as a Fluorescent Probe for Detecting Bacterial Dipeptidyl Peptidase Activities in Water-in-Oil Droplets and in Bulk.Analytical chemistry · 2022Article
- Neuropilin-2b facilitates resistance to tyrosine kinase inhibitors in non-small cell lung cancer.The Journal of thoracic and cardiovascular surgery · 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
- Fragment-based discovery of the first nonpeptidyl inhibitor of an S46 family peptidase.Scientific reports · 2019Article
- Periplasmic form of dipeptidyl aminopeptidase IV from Pseudoxanthomonas mexicana WO24: purification, kinetic characterization, crystallization and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Bacterial protease uses distinct thermodynamic signatures for substrate recognition.Scientific reports · 2017Article
- 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
- Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2015Article
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Authors and funding
16 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The dipeptidyl aminopeptidase BII (DAP BII) belongs to a serine peptidase family, S46. The amino acid sequence of the catalytic unit of DAP BII exhibits significant similarity to those of clan PA endopeptidases, such as chymotrypsin. However, the molecular mechanism of the exopeptidase activity of family S46 peptidase is unknown. Here, we report crystal structures of DAP BII. DAP BII contains a peptidase domain including a typical double β-barrel fold and previously unreported α-helical domain. The structures of peptide complexes revealed that the α-helical domain covers the active-site cleft and the side chain of Asn330 in the domain forms hydrogen bonds with the N-terminus of the bound peptide. These observations indicate that the α-helical domain regulates the exopeptidase activity of DAP BII. Because S46 peptidases are not found in mammals, we expect that our study will be useful for the design of specific inhibitors of S46 peptidases from pathogens.
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