Results 31 to 40 of about 8,679 (178)
Decoding and reprogramming fungal iterative nonribosomal peptide synthetases
Nature Communications, 2017 Nonribosomal peptides are important bioactive molecules that are synthetized by enzymes containing several catalytic domains. Here the authors describe the catalytic mechanism of fungal nonribosomal peptide synthetases and present an approach to modify ...
Dayu Yu +3 more
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Nature Communications, 2022 Nonribosomal peptide synthetases work with additional enzymes to synthesise secondary metabolites and therapeutics. Here, the authors explore bacillamide D synthesis and show the oxidase action is done while the intermediate is attached to the synthetase
Camille Marie Fortinez +5 more
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Nonribosomal Peptide Synthesis
, 2022 Nonribosomal peptides (NRPs) are a type of secondary metabolite with a wide range of pharmacological and biological activities including cytostatics, immunosuppressants or anticancer agents, antibiotics, pigments, siderophores, toxins. NRPs, unlike other proteins, are synthesized on huge nonribosomal peptide synthetase (NRPS) enzyme complexes that are ...
Sadık Dincer +2 more
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Nonribosomal Peptide Synthesis and Toxigenicity of Cyanobacteria [PDF]
Journal of Bacteriology, 1999 ABSTRACT Nonribosomal peptide synthesis is achieved in prokaryotes and lower eukaryotes by the thiotemplate function of large, modular enzyme complexes known collectively as peptide synthetases. These and other multifunctional enzyme complexes, such as polyketide synthases, are of interest due to their use in unnatural-product or ...
B A, Neilan +6 more
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Nature Communications, 2022 The catalytic domains in nonribosomal peptide synthetases (NRPSs) are responsible for a choreography of events that elongates substrates into natural products.
Jialiang Wang +9 more
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Resurrecting ancestral antibiotics: unveiling the origins of modern lipid II targeting glycopeptides
Nature Communications, 2023 Antibiotics are central to modern medicine, and yet they are mainly the products of intra and inter-kingdom evolutionary warfare. To understand how nature evolves antibiotics around a common mechanism of action, we investigated the origins of an ...
Mathias H. Hansen +8 more
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Molecular Plant-Microbe Interactions, 2006 Cyclic lipopeptides (CLPs) are versatile molecules produced by a variety of bacterial genera, including plant-associated Pseudomonas spp. CLPs are composed of a fatty acid tail linked to a short oligopeptide, which is cyclized to form a lactone ring ...
Jos M. Raaijmakers +2 more
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Engineering DNA-Templated Nonribosomal Peptide Synthesis [PDF]
Cell Chemical Biology, 2020 Abstract Nanocontainers or macromolecular scaffolds for artificial biocatalytic cascades facilitate sequential enzyme reactions but diffusive escape of intermediates limits rate enhancement. Nonribosomal peptide synthetases (NRPS) naturally form gigantic assembly lines and prevent escape by covalently tethering intermediates.
Hsin-Mei Huang +2 more
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Characterization of cereulide synthetase, a toxin-producing macromolecular machine.
PLoS ONE, 2015 Cereulide synthetase is a two-protein nonribosomal peptide synthetase system that produces a potent emetic toxin in virulent strains of Bacillus cereus.
Diego A Alonzo +2 more
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MicrobiologyOpen, 2016 Kalimantacin is an antimicrobial compound with strong antistaphylococcal activity that is produced by a hybrid trans‐acyltransferase polyketide synthase/nonribosomal peptide synthetase system in Pseudomonas fluorescens BCCM_ID9359.
Birgit Uytterhoeven +6 more
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