ArticleProceedings of the National Academy of Sciences of the United States of America2013
In vitro activity of the nisin dehydratase NisB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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67 citing papers in PubMed, 125 citations in OpenAlex.
- Biosynthesis of the Biphenomycin Family of Potent Antibiotics.Angewandte Chemie (International ed. in English) · 2025Article
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- Structural insights into the substrate binding mechanism of the class I dehydratase MadB.Communications biology · 2025Article
- Toward safer and sustainable food preservation: a comprehensive review of bacteriocins in the food industry.Bioscience reports · 2025Review
- Review
- Embleporicin: A Novel Class I Lanthipeptide from the ActinobacteriaAntibiotics (Basel, Switzerland) · 2024Article
- Insights into the production and evolution of lantibiotics from a computational analysis of peptides associated with the lanthipeptide cyclase domain.Royal Society open science · 2024Article
- PEARL-Catalyzed Peptide Bond Formation after Chain Reversal by Ureido-Forming Condensation Domains.ACS central science · 2024Article
- Cell-free biosynthesis and engineering of ribosomally synthesized lanthipeptides.Nature communications · 2024Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Recent Advances in Discovery, Bioengineering, and Bioactivity-Evaluation of Ribosomally Synthesized and Post-translationally Modified Peptides.ACS bio & med chem Au · 2023Review
- Article
- 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
- Divergent Evolution of Lanthipeptide Stereochemistry.ACS chemical biology · 2022Article
- Unexpected Methyllanthionine Stereochemistry in the Morphogenetic Lanthipeptide SapT.Journal of the American Chemical Society · 2022Article
- Analysis of Cross-Functionality within LanBTC Synthetase Complexes from Different Bacterial Sources with Respect to Production of Fully Modified Lanthipeptides.Applied and environmental microbiology · 2022Article
- A biosynthetic pathway to aromatic amines that uses glycyl-tRNA as nitrogen donor.Nature chemistry · 2022Article
- Article
7 more citing papers are in PubMed but not listed here.
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3 authors at 2 institutions in 2 countries.
Funding
Abstract
The biosynthesis of several classes of ribosomally synthesized and posttranslationally modified peptides involves dehydration of serine and threonine residues. For class I lantibiotics, thiopeptides, and goadsporin, this dehydration is catalyzed by lanthionine biosynthetic enzyme B (LanB) or LanB-like proteins. Although LanB proteins have been studied since 1992, in vitro reconstitution of their dehydration activity has been elusive. We show here the in vitro activity of the dehydratase involved in the biosynthesis of the food preservative nisin (NisB). In vitro, NisB dehydrated its substrate peptide NisA eight times in the presence of glutamate, ATP, Mg(2+), and the ribosomal/membrane fraction of bacterial cell extract. Mutation of 23 highly conserved residues of NisB identified a number of amino acids that are essential for dehydration activity. In addition, these mutagenesis studies identified three mutants, R786A, R826A, and H961A, that result in multiple glutamylations of the NisA substrate. Glutamylation was observed during both Escherichia coli coexpression of NisA with these mutants and in vitro assays. Treatment of the glutamylated substrate with WT NisB results in dehydrated NisA, suggesting that the glutamylated peptide is an intermediate in dehydration. Collectively, these studies suggest that dehydration involves glutamylation of the side chains of Ser and Thr followed by elimination. The latter step has precedent in the virginiamycin resistance protein virginiamycin B lyase. These studies will facilitate investigation of other LanB proteins involved in the biosynthesis of lantibiotics, thiopeptides, and goadsporin.
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