ArticleProceedings of the National Academy of Sciences of the United States of America2019
Zn-dependent bifunctional proteases are responsible for leader peptide processing of class III lanthipeptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 62 citations in OpenAlex.
- Diversity and Classification of the Actinopeptins: A New Family of Lanthipeptides Within the Genomes from the Phylum Actinomycetota.Antibiotics (Basel, Switzerland) · 2026Article
- A Bifunctional Protease Cleaves the Leader Peptide in the Biosynthesis of Class I Microviridins.Chembiochem : a European journal of chemical biology · 2026Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Enabling Access to Novel Bacterial Biosynthetic Potential From ONT Draft Genomic Data.Microbial biotechnology · 2025Article
- Embleporicin: A Novel Class I Lanthipeptide from the ActinobacteriaAntibiotics (Basel, Switzerland) · 2024Article
- Genome mining of sulfonated lanthipeptides reveals unique cyclic peptide sulfotransferases.Acta pharmaceutica Sinica. B · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- RiPP enzyme heterocomplex structure-guided discovery of a bacterial borosin α-RSC chemical biology · 2023Article
- Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks.Nature communications · 2023Article
- Refactoring and Heterologous Expression of Class III Lanthipeptide Biosynthetic Gene Clusters Lead to the Discovery ofACS chemical biology · 2023Article
- Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.Angewandte Chemie (International ed. in English) · 2022Article
- A scalable platform to discover antimicrobials of ribosomal origin.Nature communications · 2022Article
- Conformational remodeling enhances activity of lanthipeptide zinc-metallopeptidases.Nature chemical biology · 2022Article
- Unexpected Methyllanthionine Stereochemistry in the Morphogenetic Lanthipeptide SapT.Journal of the American Chemical Society · 2022Article
- Correlational networking guides the discovery of unclustered lanthipeptide protease-encoding genes.Nature communications · 2022Article
- Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL.Chembiochem : a European journal of chemical biology · 2021Article
- Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings.Applied and environmental microbiology · 2021Review
- Identification and characterization of andalusicin: N-terminally dimethylated class III lantibiotic fromiScience · 2021Article
- Biosynthesis and Heterologous Expression of Cacaoidin, the First Member of the Lanthidin Family of RiPPs.Antibiotics (Basel, Switzerland) · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lanthipeptides are an important subfamily of ribosomally synthesized and posttranslationally modified peptides, and the removal of their N-terminal leader peptides by a designated protease(s) is a key step during maturation. Whereas proteases for class I and II lanthipeptides are well-characterized, the identity of the protease(s) responsible for class III leader processing remains unclear. Herein, we report that the class III lanthipeptide NAI-112 employs a bifunctional Zn-dependent protease, AplP, with both endo- and aminopeptidase activities to complete leader peptide removal, which is unprecedented in the biosynthesis of lanthipeptides. AplP displays a broad substrate scope in vitro by processing a number of class III leader peptides. Furthermore, our studies reveal that AplP-like proteases exist in the genomes of all class III lanthipeptide-producing strains but are usually located outside the biosynthetic gene clusters. Biochemical studies show that AplP-like proteases are universally responsible for the leader removal of the corresponding lanthipeptides. In addition, AplP-like proteases are phylogenetically correlated with aminopeptidase N from
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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.