ArticleJournal of industrial microbiology & biotechnology2019
CylA is a sequence-specific protease involved in toxin biosynthesis.
Article in Journal of industrial microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Structure and Activity of Class II Lanthipeptides From a Thermophilic Bacterium.Chembiochem : a European journal of chemical biology · 2026Article
- Structure and Activity of Class II Lanthipeptides from a Thermophilic Bacterium.bioRxiv : the preprint server for biology · 2026Article
- S9 protease WprPCommunications chemistry · 2026Article
- Combatting virulent gut bacteria by inhibiting the biosynthesis of a two-component lanthipeptide toxin.Nature communications · 2025Article
- Substrate Specificity of a Methyltransferase Involved in the Biosynthesis of the Lantibiotic Cacaoidin.Biochemistry · 2024Article
- Bibacillin 1: A two-component lantibiotic frombioRxiv : the preprint server for biology · 2024Article
- Expression and Subcellular Localization of Lanthipeptides in Human Cells.ACS synthetic biology · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Expression of Lanthipeptides in Human Cells.bioRxiv : the preprint server for biology · 2023Article
- Maturation of subtilisin-like protease NbSLP1 from microsporidiaFrontiers in cellular and infection microbiology · 2022Article
- Structure-Activity Relationships of the Enterococcal Cytolysin.ACS infectious diseases · 2021Article
- Structural Analysis of Class I Lanthipeptides fromACS chemical biology · 2021Article
- LanCLs add glutathione to dehydroamino acids generated at phosphorylated sites in the proteome.Cell · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Article
- Probiotic Potential and Safety Evaluation ofFrontiers in microbiology · 2019Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
CylA is a subtilisin-like protein belonging to a recently expanded serine protease family related to class II lanthipeptide biosynthesis. As a leader peptidase, CylA is responsible for maturation of the enterococcal cytolysin, a lantibiotic important for Enterococcus faecalis virulence. In vitro reconstitution of CylA reveals that it accepts both linear and modified cytolysin peptides with a preference for cyclized peptides. Further characterization indicates that CylA activates itself by removing its N-terminal 95 amino acids. CylA achieves sequence-specific traceless cleavage of non-cognate peptides even if they are post-translationally modified, which makes the peptidase a powerful tool for mining novel lanthipeptides by providing a general strategy for leader peptide removal. Knowledge about the substrate specificity of CylA may also facilitate the development of protease inhibitors targeting cytolysin biosynthesis as a potential therapeutic approach for enterococcal infections.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.