Global ETD Search
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Showing 1 to 6 of 6 for “"Thiopeptide"”.
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Biochemical characterization of enzymes involved in the biosynthesis of the thiopeptide thiomuracin
… antibacterial agents with novel modes of action. Thiopeptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) that have outstanding biological profile, including high potency against a variety of antibiotic resistant pathogenic strains. Their new modes of …
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Investigating and engineering the post-translational modifications in RiPP natural product biosynthesis (I) Thiopeptides (II) Sactipeptides
… 2, 3, and 4 all elaborate further on the thiopeptide class of RiPP antibiotics. Thiopeptides typically display nanomolar activity against pathogenic Firmicutes, such as Staphylococcus aureus, Enterococcus faecalis, and Clostridium difficile. Despite their potent activity, thiopeptides …
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Mechanistic interrogations of ribosomal and non-ribosomal natural product enzymes
… (RiPPs), with a particular emphasis on the thiopeptide subclass of RiPPs. Additionally, characterization of an off-loading enzyme involved in hybrid polyketide/non-ribosomal peptide (PK-NRP) natural product biosynthesis is described.
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Post-translational modifications catalyzed by RiPP and RiPP-adjacent enzymes
… 1 focuses on a class of enzymes unique to thiopeptide biosynthesis, the pyridine synthases. These multifunctional enzymes transform a heavily modified peptide into a macrocycle through generation of a pyridine ring, through a formal [4+2]-cycloaddition, concomitant with heterocycle …
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Biomolecular NMR studies of the structure and biosynthesis of RiPP natural products
… Chapter 6 we report the discovery of two novel thiopeptide RiPPs. Genome-mining identified a minimal thiopeptide biosynthetic gene cluster with two predicted precursor peptides. These compounds were produced synthetically and chemoenzymatically and fully characterized by HRMS/MS and NMR. The …
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Practical applications of genomics to natural product discovery and biosynthesis
… aid in the structural identification of a novel thiopeptide with this post-translational modification.