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Free Piperazic Acid as a Precursor to Nonribosomal Peptides
Journal of the American Chemical Society, 2022 Piperazic acid (Piz) is a nonproteinogenic amino acid possessing a rare nitrogen–nitrogen bond. However, little is known about how Piz is incorporated into nonribosomal peptides, including whether adenylation domains specific to Piz exist. In this study,
Zi-Wang Wei +2 more
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Methods in Molecular Biology, 2023 International audienceIn this chapter, we present Norine (https://norine.univ-lille.fr/norine), the unique resource dedicated to nonribosomal peptides. First, the content of the knowledgebase and the related tools are described.
Philippe Jacques +2 more
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Nonribosomal Peptide Synthesis—Principles and Prospects
Angewandte Chemie - International Edition, 2017AbstractNonribosomal peptide synthetases (NRPSs) are large multienzyme machineries that assemble numerous peptides with large structural and functional diversity. These peptides include more than 20 marketed drugs, such as antibacterials (penicillin, vancomycin), antitumor compounds (bleomycin), and immunosuppressants (cyclosporine).
Roderich D Süssmuth, Andi Mainz
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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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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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Nonribosomal Peptides: From Genes to Products
ChemInform, 2003AbstractFor Abstract see ChemInform Abstract in Full Text.
Dirk, Schwarzer +2 more
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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 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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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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