ArticleBiopolymers2016
Characterization of the stereochemical configuration of lanthionines formed by the lanthipeptide synthetase GeoM.
Article in Biopolymers, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- 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
- An Unusual Ring Pattern in the Rosβ Lanthipeptide of the Two-Component Lantibiotic Roseocin.Journal of natural products · 2026Article
- Computational structure prediction of lanthipeptides with NMR data reveals underappreciated peptide flexibility.Protein science : a publication of the Protein Society · 2025Article
- Elucidation of the Bridging Pattern of the Lantibiotic Pseudomycoicidin.Chembiochem : a European journal of chemical biology · 2023Article
- Divergent Evolution of Lanthipeptide Stereochemistry.ACS chemical biology · 2022Article
- Unexpected Methyllanthionine Stereochemistry in the Morphogenetic Lanthipeptide SapT.Journal of the American Chemical Society · 2022Article
- Antimicrobial Potential of the GeneraAntibiotics (Basel, Switzerland) · 2022Review
- Structural Analysis of Class I Lanthipeptides fromACS chemical biology · 2021Article
- Combating Antimicrobial Resistance With New-To-Nature Lanthipeptides Created by Genetic Code Expansion.Frontiers in microbiology · 2020Review
- Article
- Heterologous biosynthesis and characterization of a glycocin from a thermophilic bacterium.Nature communications · 2019Article
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
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4 authors.
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Abstract
The biosynthesis of the class II lanthipeptide geobacillin II was reconstituted in vitro. The purified precursor peptide was modified by the lanthipeptide synthetase GeoM at temperatures ranging between 37 and 80°C demonstrating the thermostability of the enzyme. Geobacillin II shares with cytolysin, haloduracin, and carnolysin a DhxDhxXxxXxxCys motif (Dhx = dehydroalanine or dehydrobutyrine) as precursor to its N-terminal A-ring. Like in these other three lantibiotics, the lanthionine in the A-ring of geobacillin II had the LL stereochemical configuration as shown by chiral gas chromatography/mass spectrometry. Various analogues of geobacillin II were produced using co-expression of mutants of the precursor peptide GeoAII and the synthetase GeoM in Escherichia coli. The findings in this study suggest that the stereochemical outcome of the A-ring in geobacillin II is not solely dependent on the peptide sequence as previously suggested for haloduracin © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 834-842, 2016.
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