ArticleGlycobiology2017
An iterative glycosyltransferase EntS catalyzes transfer and extension of O- and S-linked monosaccharide in enterocin 96.
Article in Glycobiology, 2017. 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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13 citing papers in PubMed.
- Characterization of a novel glycocin from a thermophile.bioRxiv : the preprint server for biology · 2025Article
- Design and Biosynthesis of Ornithine 8-Containing Semaglutide Variants with a Click Chemistry-Modifiable Position 26.ACS synthetic biology · 2025Article
- Iterative glycosylation on a single residue of a mature lasso peptide.Chemical science · 2025Article
- Characterization of S-glycosylated glycocins containing three disulfides.Journal of industrial microbiology & biotechnology · 2024Article
- Review
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Structural and mechanistic investigations of protein S-glycosyltransferases.Cell chemical biology · 2021Article
- The Antimicrobial Activity of the Glycocin Sublancin Is Dependent on an Active Phosphoenolpyruvate-Sugar Phosphotransferase System.ACS infectious diseases · 2021Article
- SELECT-GLYCOCIN: a recombinant microbial system for expression and high-throughput screening of glycocins.Glycoconjugate journal · 2021Article
- IMG-ABC v.5.0: an update to the IMG/Atlas of Biosynthetic Gene Clusters Knowledgebase.Nucleic acids research · 2020Article
- Rapid Discovery of Glycocins through Pathway Refactoring in Escherichia coli.ACS chemical biology · 2018Article
- Total chemical synthesis of glycocin F and analogues:Chemical science · 2018Article
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Abstract
Glycosyltransferases are essential tools for in vitro glycoengineering. Bacteria harbor an unexplored variety of protein glycosyltransferases. Here, we describe a peptide glycosyltransferase (EntS) encoded by ORF0417 of Enterococcus faecalis TX0104. EntS di-glycosylates linear peptide of enterocin 96 - a known antibacterial, in vitro. It is capable of transferring as well as extending the glycan onto the peptide in an iterative sequential dissociative manner. It can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(β)Glc/Gal(-O/S)Ser/Thr/Cys, in one pot. Using EntS generated glycovariants of enterocin 96 peptide, size and identity of the glycan are found to influence bioactivity of the peptide. The study identifies EntS as an enzyme worth pursuing, for in vitro peptide glycoengineering.
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