Results 171 to 180 of about 526,871 (218)

Nonribosomal Peptide Synthesis—Principles and Prospects

Angewandte Chemie - International Edition, 2017
AbstractNonribosomal 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
exaly   +3 more sources

Adenylation Domains in Nonribosomal Peptide Engineering

ChemBioChem, 2019
AbstractNonribosomal 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.
Hajo Kries
exaly   +3 more sources

Nonribosomal biosynthesis of peptide antibiotics

European Journal of Biochemistry, 1990
Peptide 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
openaire   +2 more sources

Nonribosomal Peptides: From Genes to Products

ChemInform, 2003
AbstractFor Abstract see ChemInform Abstract in Full Text.
Dirk, Schwarzer   +2 more
openaire   +2 more sources

Engineering the biosynthesis of fungal nonribosomal peptides

Natural Product Reports, 2023
Fungal 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
openaire   +3 more sources

Biomimetic engineering of nonribosomal peptide synthesis

Biochemical Society Transactions, 2023
Nonribosomal 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
openaire   +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 ...
Robert Finking, Mohamed A. Marahiel
openaire   +1 more source

Introduction of a Non-Natural Amino Acid into a Nonribosomal Peptide Antibiotic by Modification of Adenylation Domain Specificity†

open access: yesAngewandte Chemie - International Edition, 2012
Calcium-dependent antibiotics (CDA) are cyclic lipopeptides assembled by nonribosomal peptide synthetase (NRPS) enzymes. Active site modification of the 3-methyl glutamate activating adenylation (A) domain of the CDA NRPS enables the incorporation of ...
Jason Micklefield   +2 more
exaly   +2 more sources

Nonribosomal biosynthesis of backbone-modified peptides

Nature Chemistry, 2017
Biosynthetic 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
openaire   +4 more sources

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