Results 11 to 20 of about 463,256 (209)
Nonribosomal Peptide Synthesis Definitely Working Out of the Rules [PDF]
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.
Stéphane Cociancich +2 more
exaly +4 more sources
Nonribosomal Peptide Synthetases in Animals [PDF]
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.
Abraham Brouwer +2 more
exaly +5 more sources
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
core +4 more sources
Engineering and elucidation of the lipoinitiation process in nonribosomal peptide biosynthesis
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 +2 more sources
Flexing and Stretching in Nonribosomal Peptide Synthetases [PDF]
Re-engineering of nonribosomal peptide synthetase molecular assembly lines has been hampered by a lack of detailed knowledge concerning inter-domain substrate transfer. Recent structural studies of catalytically relevant domain-domain interactions provide valuable insights into this problem (Liu et al., 2011; Sundlov et al., 2012 [in this issue of ...
Pfennig, Sabrina, Stubbs, Milton T.
openaire +3 more sources
(1) Background: Phytohabitans is a recently established genus belonging to rare actinomycetes. It has been unclear if its members have the capacity to synthesize diverse secondary metabolites.
Hisayuki Komaki, Tomohiko Tamura
doaj +2 more sources
Decoding and reprogramming fungal iterative nonribosomal peptide synthetases [PDF]
Nonribosomal peptides are important bioactive molecules that are synthetized by enzymes containing several catalytic domains. Here the authors describe the catalytic mechanism of fungal nonribosomal peptide synthetases and present an approach to modify ...
Dayu Yu +3 more
doaj +2 more sources
Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases [PDF]
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]
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
Synthesis of the Nonribosomal Peptide Phevalin and Analogs [PDF]
Phevalin, a cyclic nonribosomal peptide produced by Staphylococcus aureus, has intriguing biological properties. A synthetic route to access phevalin and similar pyrazinone natural products tyrvalin, leuvalin, phileucin, and a few synthetic analogs is described.
Remya Ramesh +3 more
openaire +3 more sources

