ArticleACS synthetic biology2020
High-Throughput Screening for Substrate Specificity-Adapted Mutants of the Nisin Dehydratase NisB.
Article in ACS synthetic biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Heterologous Expression and Characterization of Estercin A, a Class II Lanthipeptide Derived fromJournal of natural products · 2025Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- Article
- Functional Expression and Characterization of the Highly Promiscuous Lanthipeptide Synthetase SyncM, Enabling the Production of Lanthipeptides with a Broad Range of Ring Topologies.ACS synthetic biology · 2021Article
- Article
- Semisynthetic Macrocyclic Lipo-lanthipeptides Display Antimicrobial Activity Against Bacterial Pathogens.ACS synthetic biology · 2021Article
- Nisin- and Ripcin-Derived Hybrid Lanthipeptides Display Selective Antimicrobial Activity againstACS synthetic biology · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Brevibacillin 2V, a Novel Antimicrobial Lipopeptide With an Exceptionally Low Hemolytic Activity.Frontiers in microbiology · 2021Article
- BrevicidineB, a New Member of the Brevicidine Family, Displays an Extended Target Specificity.Frontiers in microbiology · 2021Article
- Article
- Biosynthesis of lanthionine-constrained agonists of G protein-coupled receptors.Biochemical Society transactions · 2020Review
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microbial lanthipeptides are formed by a two-step enzymatic introduction of (methyl)lanthionine rings. A dehydratase catalyzes the dehydration of serine and threonine residues, yielding dehydroalanine and dehydrobutyrine, respectively. Cyclase-catalyzed coupling of the formed dehydroresidues to cysteines forms (methyl)lanthionine rings in a peptide. Lanthipeptide biosynthetic systems allow discovery of target-specific, lanthionine-stabilized therapeutic peptides. However, the substrate specificity of existing modification enzymes impose limitations on installing lanthionines in non-natural substrates. The goal of the present study was to obtain a lanthipeptide dehydratase with the capacity to dehydrate substrates that are unsuitable for the nisin dehydratase NisB. We report high-throughput screening for tailored specificity of intracellular, genetically encoded NisB dehydratases. The principle is based on the screening of bacterially displayed lanthionine-constrained streptavidin ligands, which have a much higher affinity for streptavidin than linear ligands. The designed NisC-cyclizable high-affinity ligands can be formed via mutant NisB-catalyzed dehydration but less effectively via wild-type NisB activity. In
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