Results 171 to 180 of about 494,637 (215)
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Nonribosomal biosynthesis of peptide antibiotics
European Journal of Biochemistry, 1990Peptide antibiotics are known to contain non‐protein amino acids, D‐amino acids, hydroxy acids, and other unusual constituents. In addition they may be modified by N‐methylation and cyclization reactions. Their biosynthetic origin has been connected in many cases to an enzymatic system referred to as the ‘thiotemplate multienzymic mechanism’.
H, Kleinkauf, H, von Döhren
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Nonribosomal Peptides: From Genes to Products
ChemInform, 2003AbstractFor Abstract see ChemInform Abstract in Full Text.
Dirk, Schwarzer +2 more
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Engineering the biosynthesis of fungal nonribosomal peptides
Natural Product Reports, 2023Fungal nonribosomal peptides (NRPs) and the related polyketide–nonribosomal peptide hybrid products (PK–NRPs) are a prolific source of bioactive compounds, some of which have been developed into essential drugs.
Zhang, Liwen +6 more
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Biomimetic engineering of nonribosomal peptide synthesis
Biochemical Society Transactions, 2023Nonribosomal peptides (NRPs) have gained attention due to their diverse biological activities and potential applications in medicine and agriculture. The natural diversity of NRPs is a result of evolutionary processes that have occurred over millions of years.
Kexin Zhang, Hajo Kries
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Biosynthesis of Nonribosomal Peptides
Annual Review of Microbiology, 2004▪ Abstract Bacteria and fungi use large multifunctional enzymes, the so-called nonribosomal peptide synthetases (NRPSs), to produce peptides of broad structural and biological activity. Biochemical studies have contributed substantially to the understanding of the key principles of these modular enzymes that can draw on a much larger number of ...
Robert Finking, Mohamed A. Marahiel
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Nonribosomal biosynthesis of backbone-modified peptides
Nature Chemistry, 2017Biosynthetic modification of nonribosomal peptide backbones represents a potentially powerful strategy to modulate the structure and properties of an important class of therapeutics. Using a high-throughput assay for catalytic activity, we show here that an L-Phe-specific module of an archetypal nonribosomal peptide synthetase can be reprogrammed to ...
David L. Niquille +5 more
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Combinatorial biosynthesis of polyketides and nonribosomal peptides
Current Opinion in Chemical Biology, 2001The engineering of polyketide biosynthesis has begun to provide robust targeted libraries for screening against pharmaceutically relevant targets. New technologies that offer methodology for the rapid generation of more structurally diverse libraries have now been demonstrated.
J, Staunton, B, Wilkinson
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Nonribosomal peptide synthetases: structures and dynamics
Current Opinion in Structural Biology, 2010Nonribosomal peptide synthetases (NRPSs) are large multimodular biocatalysts that utilize complex regiospecific and stereospecific reactions to assemble structurally and functionally diverse peptides that have important medicinal applications. During this ribosome-independent peptide synthesis, catalytic domains of NRPS select, activate or modify the ...
Matthias, Strieker +2 more
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FRET monitoring of a nonribosomal peptide synthetase
Nature Chemical Biology, 2017Nonribosomal peptide synthetases (NRPSs) are multidomain enzyme templates for the synthesis of bioactive peptides. Large-scale conformational changes during peptide assembly are obvious from crystal structures, yet their dynamics and coupling to catalysis are poorly understood.
Jonas Alfermann +8 more
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A Practical Guideline to Engineering Nonribosomal Peptide Synthetases
2023The bioengineering of nonribosomal peptide synthetases (NRPSs) is a rapidly developing field to access natural product derivatives and new-to-nature natural products like scaffolds with changed or improved properties. However, the rational (re-)design of these often gigantic assembly-line proteins is by no means trivial and needs in-depth insights into
Abbood, N. +3 more
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