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Free Piperazic Acid as a Precursor to Nonribosomal Peptides
Journal of the American Chemical Society, 2022Piperazic 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,
Raymond Andersen +2 more
exaly +2 more sources
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 ...
Mohamed A Marahiel
exaly +2 more sources
Nonribosomal biosynthesis of backbone-modified peptides.
Nature Chemistry, 2018Biosynthetic 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
semanticscholar +4 more sources
Pseudoaeruginosins, nonribosomal peptides in Nodularia spumigena.
ACS Chemical Biology, 2015Nodularia spumigena is a filamentous cyanobacterium that forms toxic blooms in brackish waters around the world through the production of the pentapeptide toxin nodularin. This cyanobacterium also produces large amounts of protease inhibitors belonging to the aeruginosin and spumigin families. Here we report the discovery of previously unknown protease
Liwei Liu +9 more
semanticscholar +3 more sources
Bioinformatics Tools for the Discovery of New Nonribosomal Peptides.
Methods in molecular biology, 2016This chapter helps in the use of bioinformatics tools relevant to the discovery of new nonribosomal peptides (NRPs) produced by microorganisms. The strategy described can be applied to draft or fully assembled genome sequences. It relies on the identification of the synthetase genes and the deciphering of the domain architecture of the nonribosomal ...
V. Leclère +3 more
semanticscholar +6 more sources
2009
Nonribosomal peptides are a diverse group of compounds synthesized via modular nonribosomal peptide synthetase (NRPS) enzyme complexes. They are produced by a variety of prokaryotes, including streptomycetes, bacillus, and cyanobacteria, and lower-order eukaryotes such as fungi and sponges.
Roberts, Alexandra A. +2 more
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Nonribosomal peptides are a diverse group of compounds synthesized via modular nonribosomal peptide synthetase (NRPS) enzyme complexes. They are produced by a variety of prokaryotes, including streptomycetes, bacillus, and cyanobacteria, and lower-order eukaryotes such as fungi and sponges.
Roberts, Alexandra A. +2 more
openaire +3 more sources
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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Journal of the American Chemical Society
Nonribosomal peptides serve as pivotal sources for drug discovery. Accurate prediction of the substrate specificity of adenylation domains in nonribosomal peptide synthetases is crucial for genome mining of nonribosomal peptides, yet current prediction ...
Zhihan Zhang +8 more
semanticscholar +1 more source
Nonribosomal peptides serve as pivotal sources for drug discovery. Accurate prediction of the substrate specificity of adenylation domains in nonribosomal peptide synthetases is crucial for genome mining of nonribosomal peptides, yet current prediction ...
Zhihan Zhang +8 more
semanticscholar +1 more source