Results 11 to 20 of about 8,679 (178)

Nonribosomal Peptide Synthetases in Animals. [PDF]

open access: yesGenes (Basel), 2023
Nonribosomal peptide synthetases (NRPSs) are a class of cytosolic enzymes that synthesize a range of bio-active secondary metabolites including antibiotics and siderophores. They are widespread among both prokaryotes and eukaryotes but are considered rare among animals.
Suring W   +5 more
europepmc   +4 more sources

Nonribosomal Peptide Synthesis Definitely Working Out of the Rules [PDF]

open access: yesMicroorganisms, 2022
Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields.
Matthieu Duban   +2 more
doaj   +2 more sources

Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases [PDF]

open access: yesMarine Drugs
Nonribosomal peptides (NRPs) are biosynthesized by nonribosomal peptide synthetases (NRPSs) and are widely distributed in both terrestrial and marine organisms. Many NRPs and their analogs are biologically active and serve as therapeutic agents.
Mengli Zhang   +5 more
doaj   +2 more sources

Development of a chemical scaffold for inhibiting nonribosomal peptide synthetases in live bacterial cells [PDF]

open access: yesBeilstein Journal of Organic Chemistry
The adenylation (A) domain is essential for non-ribosomal peptide synthetases (NRPSs), which synthesize various peptide-based natural products, including virulence factors, such as siderophores and genotoxins.
Fumihiro Ishikawa   +3 more
doaj   +2 more sources

Discovery of Acyl-Surugamide A2 from Marine Streptomyces albidoflavus RKJM-0023—A New Cyclic Nonribosomal Peptide Containing an N-ε-acetyl-L-lysine Residue [PDF]

open access: yesMolecules
We report the discovery of a novel cyclic nonribosomal peptide (NRP), acyl-surugamide A2, from a marine-derived Streptomyces albidoflavus RKJM-0023 (CP133227).
Zacharie A. Maw   +5 more
doaj   +2 more sources

BioCAT: Search for biosynthetic gene clusters producing nonribosomal peptides with known structure

open access: yesComputational and Structural Biotechnology Journal, 2022
Nonribosomal peptides are a class of secondary metabolites synthesized by multimodular enzymes named nonribosomal peptide synthetases and mainly produced by bacteria and fungi.
Dmitry N. Konanov   +3 more
doaj   +1 more source

A Nonribosomal System of Peptide Biosynthesis [PDF]

open access: yesEuropean Journal of Biochemistry, 1996
This review covers peptide structures originating from the concerted action of enzyme systems without the direct participation of nucleic acids. Biosynthesis proceeds by formation of linear peptidyl intermediates which may be enzymatically modified as well as transformed into specific cyclic structures.
H, Kleinkauf, H, Von Döhren
openaire   +2 more sources

Biosynthetic Functionalization of Nonribosomal Peptides

open access: yesJournal of the American Chemical Society, 2021
Nonribosomal peptides (NRPs) are a therapeutically important class of secondary metabolites that are produced by modular synthetases in assembly-line fashion. We previously showed that a single Trp-to-Ser mutation in the initial Phe-loading adenylation domain of tyrocidine synthetase completely switches the specificity toward clickable analogues.
David L. Niquille   +3 more
openaire   +3 more sources

Genomic and Chemical Diversity of Bacillus subtilis Secondary Metabolites against Plant Pathogenic Fungi

open access: yesmSystems, 2021
Bacillus subtilis produces a wide range of secondary metabolites providing diverse plant growth-promoting and biocontrol abilities. These secondary metabolites include nonribosomal peptides with strong antimicrobial properties, causing either cell lysis,
Heiko T. Kiesewalter   +10 more
doaj   +1 more source

Engineering and elucidation of the lipoinitiation process in nonribosomal peptide biosynthesis

open access: yesNature Communications, 2021
Nonribosomal lipopeptides contain an acyl chain important for bioactivity, but its incorporation into the peptidyl backbone, mediated by the starter condensation (Cs) domain of nonribosomal peptide synthases, is not fully understood.
Lin Zhong   +10 more
doaj   +1 more source

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