Results 51 to 60 of about 5,756 (191)

Antifungal peptides in marine invertebrates [PDF]

open access: yesInvertebrate Survival Journal, 2010
A majority of terrestrial and marine organisms use to fend off a wide range of microorganisms, including bacteria and fungi by employing “antimicrobial peptides (AMPs)” that are ribosomally synthesized from proteinogenic amino acids.
N Fusetani
doaj  

Piecing together nonribosomal peptide synthesis

open access: yesCurrent Opinion in Structural Biology, 2018
Nonribosomal peptide synthetases (NRPSs) produce peptide products with wide-ranging biological activities. NRPSs are macromolecular machines with modular assembly-line logic, a complex catalytic cycle, moving parts and multiple active sites. They are organized into repeating sets of domains, called modules.
Reimer, Janice M.   +3 more
openaire   +3 more sources

Biologically Active Nonribosomal Peptides. II. Nonribosomal Peptides of Various Biological Action

open access: yesАнтибиотики и Химиотерапия, 2020
The second part of the review concerned with investigation of nonribosomal peptides.
T. I. Orlova   +2 more
doaj  

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

Dissecting and Exploiting Nonribosomal Peptide Synthetases

open access: yesActa Biochimica et Biophysica Sinica, 2004
A large number of therapeutically useful cyclic and linear peptides of bacteria or fungal origin are synthesized via a template-directed, nucleic-acid-independent nonribosomal mechanism. This process is carried out by mega-enzymes called nonribosomal peptide synthetases (NRPSs).
Qing-Tao, Shen   +3 more
openaire   +2 more sources

Discovery and Biosynthesis of the Novel Glycotetrapeptide Antibiotic Biffamycin A

open access: yesAngewandte Chemie, Volume 138, Issue 26, 22 June 2026.
Genetic de‐regulation of a silent biosynthetic pathway allowed isolation and characterisation of a novel glycopeptide antibiotic named biffamycin A, which harbours unprecedented 5‐chloro‐4‐methoxy tryptophan and 3R‐hydroxy(α‐D‐mannoysl)‐D‐lysine moieties and is bioactive against MRSA and VRSA.
Michael W. Brigham   +11 more
wiley   +2 more sources

Cell-free synthetic biology for in vitro biosynthesis of pharmaceutical natural products

open access: yesSynthetic and Systems Biotechnology, 2018
Natural products with significant biological activities continuously act as rich sources for drug discovery and development. To harness the potential of these valuable compounds, robust methods need to be developed for their rapid and sustainable ...
Jian Li, Lingkai Zhang, Wanqiu Liu
doaj   +1 more source

The insect pathogen Serratia marcescens Db10 uses a hybrid non-ribosomal peptide synthetase-polyketide synthase to produce the antibiotic althiomycin [PDF]

open access: yes, 2012
There is a continuing need to discover new bioactive natural products, such as antibiotics, in genetically-amenable micro-organisms. We observed that the enteric insect pathogen, Serratia marcescens Db10, produced a diffusible compound that inhibited the
Coulthurst Sarah J.   +28 more
core   +1 more source

Identification of a Nonribosomal Peptide Analog With Activity Against Multiple Gram‐Positive Bacteria via a Synthetic Bioinformatic Natural Product Discovery Approach

open access: yesAdvanced Science, EarlyView.
The genome of Rhodococcus erythropolis D‐1 was analyzed by bioinformatic tools to mine a novel nonribosomal peptide synthetase (NRPS) gene cluster. A nonribosomal peptide analog ZURJC5 associated with the NRPS was chemically synthesized. Through structure‐activity relationship studies, ZURJC28 was ultimately obtained and showed antibacterial activity ...
Keyi Chen   +9 more
wiley   +1 more source

Norine: update of the nonribosomal peptide resource.

open access: yesNucleic acids research, 2019
Norine, the unique resource dedicated to nonribosomal peptides (NRPs), is now updated with a new pipeline to automate massive sourcing and enhance annotation. External databases are mined to extract NRPs that are not yet in Norine. To maintain a high data quality, successive filters are applied to automatically validate the NRP annotations and only ...
Flissi, Areski   +10 more
openaire   +5 more sources

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