ArticleApplied and environmental microbiology2019
Mechanistic Insight into the Binding and Swelling Functions of Prepeptidase C-Terminal (PPC) Domains from Various Bacterial Proteases.
Article in Applied and environmental microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Thermostable Bacterial Collagenolytic Proteases: A Review.Journal of microbiology and biotechnology · 2024Review
- Mobile genetic elements used by competing coral microbial populations increase genomic plasticity.The ISME journal · 2022Article
- Mechanistic Insight into the Fragmentation of Type I Collagen Fibers into Peptides and Amino Acids by aApplied and environmental microbiology · 2022Article
- Maturation Process and Characterization of a Novel Thermostable and Halotolerant Subtilisin-Like Protease with High Collagenolytic Activity but Low Gelatinolytic Activity.Applied and environmental microbiology · 2022Article
- Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.Nature communications · 2022Article
- Characterization of a New M4 Metalloprotease With Collagen-Swelling Ability From MarineFrontiers in microbiology · 2020Article
- Purification, Characterization, and Application for Preparation of Antioxidant Peptides of Extracellular Protease fromMolecules (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial prepeptidase C-terminal (PPC) domain can be found in the C termini of a wide variety of proteases that are secreted by marine bacteria. However, the functions of these PPC domains remain unknown due to a lack of systematic research. Here, the binding and swelling abilities of eight PPC domains from six different proteases were compared systematically via scanning electron microscopy (SEM), enzyme assays, and fluorescence spectroscopy. These PPC domains all possess the ability to bind and swell insoluble collagen. PPC domains can expose collagen monomers but cannot disrupt the pyridinoline cross-links or unwind the collagen triple helix. This ability can play a synergistic role alongside collagenase in collagen hydrolysis. Site-directed mutagenesis of the PPC domain from
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