Results 31 to 40 of about 10,782 (215)
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
openaire +1 more source
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
openaire +2 more sources
Antibacterial Property Of A Coral-Associated Bacterium Pseudoalteromonas Luteoviolacea Against Shrimp Pathogenic Vibrio Harveyi(In Vitro Study) [PDF]
, 2004 A coral-associated bacterium was successfully screened for secondary metabolites production based on PCR amplification of the non-ribosomal peptide synthetase gene and was identified as closely related to Pseudoalteromonas luteoviolacea based on its 16S ...
TORBEN MARTENS +19 more
core +1 more source
Rapid Peptide Cyclization Inspired by the Modular Logic of Nonribosomal Peptide Synthetases. [PDF]
J Am Chem SocNonribosomal cyclic peptides (NRcPs) are structurally complex natural products and a vital pool of therapeutics, particularly antibiotics. Their structural diversity arises from the ability of the multidomain enzyme assembly lines, nonribosomal peptide ...
Ding Y +12 more
europepmc +3 more sources
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
doaj +1 more source
The role of the phosphopantetheinyltransferase enzyme, PswP, in the biosynthesis of antimicrobial secondary metabolites by Serratia marcescens Db10 [PDF]
, 2014 Phosphopantetheinyl transferase (PPTase) enzymes fulfil essential roles in primary and secondary metabolism in prokaryotes, archaea and eukaryotes. PPTase enzymes catalyse the essential modification of the carrier protein domain of fatty acid synthases ...
Gerc, Amy J. +2 more
core +1 more source
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
doaj +1 more source
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
openaire +2 more sources
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
doaj +1 more source