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ProteomicsCharacterization of the Clostridioides difficile 630Δerm putative Pro-Pro endopeptidase CD1597
Clostridioides difficile is the leading cause of antibiotic-associated infections worldwide. Within the host, C. difficile can transition from a sessile to a motile state by secretion of PPEP-1, which releases the cells from the intestinal epithelium by cleaving adhesion proteins. PPEP-1 belongs to ...
ORGANISM(S): Peptoclostridium difficile (strain 630) (Clostridium difficile) 
2024-05-27 | PXD052347 | Pride
Tmtpro Proteomics Sporulation Clostridioides difficile Proteases Pro-pro endopeptidases 
ProteomicsIn-depth specificity profiling of Pro-Pro endopeptidases (PPEPs) using combinatorial synthetic peptide libraries
Proteases comprise the class of enzymes that catalyze the hydrolysis of peptide bonds, thereby playing a pivotal role in many aspects of life. The amino acids surrounding the scissile bond determine the susceptibility towards protease-mediated hydrolysis. A detailed understanding of the cleavage spe...
ORGANISM(S): Paenibacillus alvei DSM 29 Geobacillus stearothermophilus Clostridioides difficile 
2023-08-01 | PXD038277 | Pride
Pro-pro endopeptidase Specificity profiling Mass spectrometry (ms) Ppep Synthetic peptide libraries Substrate specificity High-performance liquid chromatography (hplc) Fret peptides Metalloprotease 
ProteomicsNon-prime- and Prime-side Profiling of Pro-Pro Endopeptidase Specificity Using Synthetic Combinatorial Peptide Libraries and Mass Spectrometry
A group of bacterial proteases, the Pro-Pro endopeptidases (PPEPs), possess the unique ability to hydrolyze proline-proline bonds in proteins. Since a protease’s function is largely determined by its substrate specificity, methods that can extensively characterize substrate specificity are valuable ...
ORGANISM(S): Anoxybacillus tepidamans Paenibacillus alvei Peptoclostridium difficile (strain 630) (Clostridium difficile) 
2025-11-11 | PXD050236 | Pride
Clostridioides difficile Paenibacillus alvei Ppep Protease Specificity Pro-pro endopeptidase Anoxybacillus tepidamans Lc-ms/ms 
ProteomicsBiochemical and structural characterization of PPEP-3 from Geobacillus thermodenitrificans
The members of the group of Pro-Pro endopeptidases (PPEPs) are secreted bacterial endoproteases that display a unique preference for hydrolyzing their substrates between two proline residues. The active site cleft of PPEPs accommodates the six substrate residues P3 to P3’, and the interactions betwe...
ORGANISM(S): Geobacillus thermodenitrificans 
2025-11-11 | PXD061585 | Pride
Geobacillus thermodenitrificans Macromolecular x-ray crystallography Zinc metallopeptidase Mass spectrometry Substrate specificity Pro-pro endopeptidase-3 
UnknownComparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue.
Not available
S-EPMC1134072 | biostudies-literature
UnknownStructural analyses and substrate profiling of PPEP-3 provide new insights into the molecular basis of Pro-Pro endopeptidase specificity.
Not available
S-EPMC12828418 | biostudies-literature
UnknownCharacterization of the Clostridioides difficile 630Δerm putative Pro-Pro endopeptidase CD1597.
Not available
S-EPMC11460543 | biostudies-literature
UnknownDiscovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.
Not available
S-EPMC6052223 | biostudies-literature
UnknownPhylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.
Not available
S-EPMC8610288 | biostudies-literature
UnknownA Dual-Enzyme Amplification Loop for the Sensitive Biosensing of Endopeptidases.
Not available
S-EPMC10357553 | biostudies-literature
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