• Publications
  • Influence
Caulosegnins I-III: a highly diverse group of lasso peptides derived from a single biosynthetic gene cluster.
The structure of the most abundant lasso peptide caulosegnin I is elucidated via NMR spectroscopic analysis and a thorough mutational analysis is performed that gave insight into their biosynthesis and revealed important factors affecting the stabilization of the lasso fold in general. Expand
The astexin-1 lasso peptides: biosynthesis, stability, and structural studies.
A new lasso structure with a tight loop and long tail as well as narrow specificity of the maturation machinery for some essential residues associated with the protease processing site, involved in macrolactam ring formation and entrapment of the tail is revealed. Expand
Lasso peptides: an intriguing class of bacterial natural products.
The newest findings about the lasso peptides, an emerging class of ribosomally assembled and post-translationally modified peptides from bacteria that were first described in 1991 are discussed and the general methodology to elucidate these structures by NMR will be discussed and pitfalls for these approaches are highlighted. Expand
Lasso peptides from proteobacteria: Genome mining employing heterologous expression and mass spectrometry.
A B protein-centric genome mining approach is demonstrated through which it is able to identify 102 putative lasso peptide biosynthetic gene clusters from a total of 87 different proteobacterial strains. Expand
The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
It is revealed that ThnB is a radical S‐adenosylmethionine (SAM) enzyme containing two [4Fe–4S] clusters and it is shown that the PqqD homologous N‐terminal domain of Thn B is essential for maturation of the thurincin H precursor peptide, but not for the SAM cleavage activity of ThNB. Expand
Xanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ring.
Lasso peptides belong to the class of ribosomally synthesized and post-translationally modified peptides. Their common distinguishing feature is an N-terminal macrolactam ring that is threaded by theExpand
Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin*
The study reveals how lasso peptides are chemically diversified and sets the foundation for rational engineering of these intriguing natural products. Expand
Enterobacter bugandensis: a novel enterobacterial species associated with severe clinical infection
It is demonstrated that the extended spectrum ß-lactam producing isolate EB-247 is highly virulent in both Galleria mellonella and mouse models of infection and as efficient as Salmonella Typhimurium in inducing systemic infection and release of proinflammatory cytokines. Expand
Characterization of caulonodin lasso peptides revealed unprecedented N-terminal residues and a precursor motif essential for peptide maturation
Lasso peptides, a peculiar family of ribosomally assembled and post-translationally modified peptides (RiPPs), possess a fascinating 3D structure, which can confer rigidity and stability againstExpand
Factors Governing the Thermal Stability of Lasso Peptides
  • J. Hegemann
  • Chemistry, Medicine
  • Chembiochem : a European journal of chemical…
  • 15 January 2020
The current state of understanding the physicochemical parameters deciding the fate of a lasso peptide at elevated temperatures is discussed, and an overview is given of the techniques developed to streamline the separation and discrimination ofLasso peptides from their branched‐cyclic topoisomers. Expand