Lantibiotika‐Kongenere mit nicht‐kanonischen Aminosäuren durch ribosomale In‐vivo‐Peptidsynthese

Oldach, Florian; Toma, Rashed Al; Kuthning, Anja; Caetano, Tânia; Mendo, Sónia; Budiša, Nediljko

doi:10.1002/ange.201106154

Cited by 17 publications

(1 citation statement)

References 32 publications

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“…3 In addition, the ribosomal origin of these peptides4 facilitates structure engineering studies in the native producer5 or in a heterologous host 6. 7 Recently we reported on the structures and biosynthetic gene cluster ( lab ) of labyrinthopeptins, protagonists of the emerging group of class III lantibiotics 8. In addition to unique antiallodynic and antiretroviral activities, a novel structural variation of lanthionine was identified, namely labionin (Lab).…”

Section: Introductionmentioning

confidence: 99%

Curvopeptin: A New Lanthionine‐Containing Class III Lantibiotic and its Co‐substrate Promiscuous Synthetase

Krawczyk

Völler

et al. 2012

ChemBioChem

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Lantibiotics are ribosomally synthesized peptides containing post-translationally installed lanthionine thioether bridges. Recently characterized class III lantibiotics have also revealed the occurrence of labionin, a novel carbacyclic variation of lanthionine, and highlighted the structural diversity within this group. Here we describe the discovery and characterization of curvopeptins produced by Thermomonospora curvata, the first class III lantibiotics of thermophilic origin. Furthermore, investigation of the modifying enzyme CurKC and in particular the characterization of its specificity toward phosphorylation co-substrates was performed. Remarkably, all investigated NTPs and dNTPs were accepted by the enzyme, although the purine nucleotides ATP/dATP and GTP/dGTP were the preferred co-substrates. This finding complements previous studies on the class III lantibiotic synthetases LabKC and EryKC and underlines the surprising promiscuity of the Ser/Thr-kinase domain. Enzymatic studies with a precursor peptide mutant allowed the assignment of all dehydration sites and further GC-MS analysis revealed the presence of lanthionine as the main type of intramolecular ring.

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Section: Introductionmentioning

confidence: 99%

Curvopeptin: A New Lanthionine‐Containing Class III Lantibiotic and its Co‐substrate Promiscuous Synthetase

Krawczyk

Völler

et al. 2012

ChemBioChem

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Cyclization of Peptides by using Selenolanthionine Bridges

et al. 2012

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Nicht‐ribosomale Peptidsynthese – Prinzipien und Perspektiven

Süßmuth

Mainz

2017

Angewandte Chemie

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Nicht‐ribosomale Peptidsynthetasen (NRPSs) sind große Multienzymmaschinerien, die zahlreiche Peptide mit enormer struktureller und funktionaler Diversität erzeugen. Unter diesen Produkten befinden sich mehr als 20 auf dem Markt befindliche Wirkstoffe, darunter Antibiotika (Penicillin, Vancomycin), antitumorale Medikamente (Bleomycin) und Immunsuppressiva (Cyclosporin). In den vergangenen Jahrzehnten haben biochemische sowie strukturbiologische Studien mechanistische Einblicke in die hochkomplexen NRPSs gewährt. Dieser Aufsatz fasst den aktuellen Kenntnisstand über die zugrundeliegenden Mechanismen von NRPSs zusammen und gibt einen Überblick über die Vielfalt ihrer Produkte. Ebenso behandelt werden die Probleme und Herausforderungen, die mit der Umprogrammierung von NRPS‐Systemen einhergehen. Das Potenzial einer solchen Umprogrammierung liegt begründet in einer nachhaltigen Generierung von Wirkstoffanaloga und neuen Substanzbibliotheken, die anderenfalls kaum zugänglich sind.

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Lantibiotika‐Kongenere mit nicht‐kanonischen Aminosäuren durch ribosomale In‐vivo‐Peptidsynthese

Cited by 17 publications

References 32 publications

Curvopeptin: A New Lanthionine‐Containing Class III Lantibiotic and its Co‐substrate Promiscuous Synthetase

Curvopeptin: A New Lanthionine‐Containing Class III Lantibiotic and its Co‐substrate Promiscuous Synthetase

Cyclization of Peptides by using Selenolanthionine Bridges

Nicht‐ribosomale Peptidsynthese – Prinzipien und Perspektiven

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