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Correction to: Characterization and catalytic investigation of fungal single-module nonribosomal peptide synthetase in terpene-amino acid meroterpenoid biosynthesis. [PDF]
J Ind Microbiol Biotechnoleuropepmc +1 more source
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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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Adenylation Domains in Nonribosomal Peptide Engineering
ChemBioChem, 2019AbstractNonribosomal peptides are a prolific source of bioactive molecules biosynthesized on large, modular assembly line synthetases. Synthetic biologists seek to obtain tailored peptides with tuned or novel bioactivities by engineering modules and domains of these nonribosomal peptide synthetases.
Aleksa Stanisic, Hajo Kries
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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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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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Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis
Chemical Reviews, 1997Mohamed A Marahiel +2 more
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