Results 61 to 70 of about 8,679 (178)
ABSTRACT Cyanobacterial harmful algal blooms (cyanoHABs) threaten human, animal, and ecosystem health and safety through production of toxic secondary metabolites. Microcystis, a cosmopolitan bloom‐forming cyanobacterial genus, is well‐known for producing hepatotoxic microcystins (MCs), but it can produce many other bioactive cyanopeptides, such as ...
Lauren N. Hart +7 more
wiley +1 more source
Automated genome mining for natural products
Background Discovery of new medicinal agents from natural sources has largely been an adventitious process based on screening of plant and microbial extracts combined with bioassay-guided identification and natural product structure elucidation ...
Zajkowski James +4 more
doaj +1 more source
Taxonomic Positions of a Nyuzenamide-Producer and Its Closely Related Strains
Streptomyces sp. N11-34 is a producer of bicyclic peptides named nyuzenamides A and B. We elucidated its taxonomic position and surveyed its nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) gene clusters by whole genome analysis ...
Hisayuki Komaki +2 more
doaj +1 more source
Caffeic acid is a central metabolite in the fungal bioluminescence pathway. We identified and characterized caffeylpyruvate hydrolase from Neonothopanus gardneri (ngarCPH) and demonstrate its ability to hydrolyze fungal oxyluciferin into caffeic and pyruvic acids, confirming a complete and self‐sustained fungal bioluminescence cycle.
Caio K. Zamuner +8 more
wiley +1 more source
Streptomyces sp. N11-50 was isolated from deep-sea water and found to produce diketopiperazine (DKP) compounds such as albonoursin and cyclo(Phe-Leu).
Hisayuki Komaki +2 more
doaj +1 more source
The third part of the review is concerned with investigation of nonribosomal peptides.
T. I. Orlova +2 more
openaire +2 more sources
Structural Biology of Nonribosomal Peptide Synthetases [PDF]
The nonribosomal peptide synthetases are modular enzymes that catalyze synthesis of important peptide products from a variety of standard and non-proteinogenic amino acid substrates. Within a single module are multiple catalytic domains that are responsible for incorporation of a single residue. After the amino acid is activated and covalently attached
Bradley R, Miller, Andrew M, Gulick
openaire +2 more sources
The tryptophan prenyltransferase ComQ from Bacillus subtilis 168 can prenylate daptomycin at Trp1
ComQ168 from Bacillus subtilis 168 catalyzes C‐terminal tryptophan farnesylation of ComX to generate a competence‐inducing pheromone. Recombinant ComQ168 also modifies cyclic peptides, including Daptomycin, likely at the N‐terminal tryptophan. Structural modeling highlights a C‐terminal binding region, supporting substrate promiscuity and establishing ...
Yanli Xu +2 more
wiley +1 more source
NocTE is a nonribosomal peptide synthetase thioesterase that completes the biosynthesis of pro-nocardicin G, the precursor for nocardicin β-lactam antibiotics. Here the authors provide mechanistic insights into NocTE by determining its crystal structures
Ketan D. Patel +5 more
doaj +1 more source
Norine: A powerful resource for novel nonribosomal peptide discovery
Since its first release in 2008, Norine remains the unique resource completely devoted to nonribosomal peptides (NRPs). They are very attractive microbial secondary metabolites, displaying a remarkable diversity of structure and functions. Norine (http://
M. Pupin +5 more
doaj +1 more source

