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Non-Ribosomal Peptide Synthetases of Fungi
2009Non-ribosomal peptide synthetases (NRPSs) are large enzymes which catalyze the assembly of a vast number of complex peptides which often possess interesting properties. The physiological role of non-ribosomally produced peptides is discussed and the organization of NRPSs in fungi is described.
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A dissected non-ribosomal peptide synthetase maintains activity
Biochimica et Biophysica Acta (BBA) - Proteins and ProteomicsNon-ribosomal peptide synthetases (NRPSs) generate chemically complex compounds and their modular architecture suggests that changing their domain organization can predictably alter their products. Ebony, a small three-domain NRPS, catalyzes the formation of β-alanine containing amides from biogenic amines.
Amanda J, Platt +3 more
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Total synthesis and functional analysis of non‐ribosomal peptides
The Chemical Record, 2011AbstractAntillatoxin and polytheonamide B are cytotoxic non‐ribosomal peptides, both isolated from marine sources. These molecules possess unique biological activities that relate to ion channel proteins. Antillatoxin binds and activates voltage‐gated sodium channels, while polytheonamide mimics functions of an ion channel protein.
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[Biosynthesis of peptides: a non-ribosomal system].
Die Naturwissenschaften, 1992The biosynthesis of peptides in nonribosomal systems is accomplished by complex multienzymes. These multienzymes assemble the required template for the construction of each natural product in the form of linearly coupled modules. This organization principle permits the integration of multistep synthetic processes on a single macromolecule.
H, Kleinkauf +3 more
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Non-ribosomal peptide formation on multifunctional proteins
Trends in Biochemical Sciences, 1983Abstract Polyenzymes have been found to catalyse the formation of peptides containing non-protein constituents. Such protein templates are multifunctional polypeptides with catalytic sites for amino acid activation, epimerization, modification, peptide elongation and cyclization reactions.
H. Kleinkauf, H. von Do¨hren
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3.7.1 Isoprenoids, Polyketides, and (Non)ribosomal Peptides
2015AbstractThis chapter describes methods for the biosynthesis and biocatalysis of natural products belonging to the isoprenoids, polyketides (acetate pathway), phenylpropanoids (shikimate pathway), alkaloids, and ribosomal and nonribosomal peptides. Recent advances in genome-sequencing technologies and synthetic biology approaches are discussed, and ...
M. Quin +3 more
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[Advances in engineering non-ribosomal peptide synthetase].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2021Non-ribosomal peptide synthetases catalyze the biosynthesis of structurally and functionally diverse non-ribosomal peptide natural products, which have broad applications in pharmaceutical, agricultural, and industrial sectors. Engineered non-ribosomal peptide synthetases can be used to produce novel non-ribosomal peptides through combinatorial ...
Chen, Wang, Yuquan, Xu
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Non-ribosomal Peptides from Entomogenous Fungi
2015Entomogenous fungi play a very important role in controlling the natural population of insect pests. Many of them have been developing as myco-insecticides. During evolution, entomogenous fungi acquired lots of pathogenic factors against host insects. Non-ribosomal peptide (NRP) is a usual pathogenic factor of entomogenous fungi.
Qiongbo Hu, Tingyan Dong
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Peptide Bond Formation in Non-ribosomal Systems
1978Biosynthesis of peptides requires (1) carboxyl group activation, and (2) specific addition of acceptor amino (imino) group. Activation reactions include formation of phosphates (peptidoglycan, glutathione) or of adenylates (aminoacyl-tRNA-ligases, gramicidin S-synthetase).
H. Kleinkauf, H. Koischwitz
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Non-ribosomal peptide biosynthetic systems
2002The increasing number of pathogenic organisms developing resistance to traditional therapy requires novel concepts for the generation of pharmacologically useful drugs. A wide variety of natural peptides, peptidolactones, and depsipeptides, are synthesised non-ribosomally with the aid of multifunctional peptide synthetases. Several hundred compounds of
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