ReviewWorld journal of microbiology & biotechnology2025
Promiscuity of lanthipeptide enzymes: new challenges and applications.
Review in World journal of microbiology & biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Diversity and Classification of the Actinopeptins: A New Family of Lanthipeptides Within the Genomes from the Phylum Actinomycetota.Antibiotics (Basel, Switzerland) · 2026Article
- Heterologous expression reveals a cryptic morphogenetic lanthipeptide durhapeptin from Streptomyces durhamensis.Antonie van Leeuwenhoek · 2026Article
- Unexplored biosynthetic gene clusters in bacteria isolated from Brazilian stingless bee honey with activity against multidrug-resistant pathogens.Current research in microbial sciences · 2026Article
- LanthMS: A Computational Tool for the Structure Elucidation of Lanthipeptides from Tandem Mass Spectrometry Data.Protein and peptide letters · 2026Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lanthipeptides are a group of peptides synthesized by ribosomes that undergo post-translational modifications and have significant potential for medical and biotechnological applications. Various bacterial strains produce these peptides, and their synthesis involves the structural modification of precursor compounds through specialized enzymes present within a biosynthetic gene cluster (BGC) of the producing organisms. These enzymes are particularly notable for their capacity to modify non-cognate substrates, allowing for the installation of lanthionine rings on precursor peptides and enabling further modifications, such as methylation, reduction, and oxidation, to enhance the biological properties of specific peptides. The inherent flexibility of lanthipeptide enzymes-an important characteristic of this class of proteins-can be utilized to create peptides with improved bioactive and physicochemical properties. This review synthesizes recent advances in the application of promiscuous enzymes for the synthesis of bioactive peptides, emphasizing the diverse classes identified to date.
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Registered trials
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.