Results 31 to 40 of about 557,797 (165)

Distinct roles for intra- and extracellular siderophores during Aspergillus fumigatus infection.

open access: yesPLoS Pathogens, 2007
Siderophore biosynthesis by the highly lethal mould Aspergillus fumigatus is essential for virulence, but non-existent in humans, presenting a rare opportunity to strategize therapeutically against this pathogen.
Markus Schrettl   +9 more
doaj   +1 more source

Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions

open access: yesNature Communications, 2019
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

Genetic and functional characterization of the gene cluster directing the biosynthesis of putisolvin I and II in Pseudomonas putida strain PCL1445 [PDF]

open access: yes, 2008
Pseudomonas putida PCL1445 secretes two cyclic lipopeptides, putisolvin I and putisolvin II, which possess a surface-tension-reducing ability, and are able to inhibit biofilm formation and to break down biofilms of Pseudomonas species including ...
Dubern, J.F.   +7 more
core   +1 more source

Systematic analysis of the kalimantacin assembly line NRPS module using an adapted targeted mutagenesis approach

open access: yesMicrobiologyOpen, 2016
Kalimantacin is an antimicrobial compound with strong antistaphylococcal activity that is produced by a hybrid trans‐acyltransferase polyketide synthase/nonribosomal peptide synthetase system in Pseudomonas fluorescens BCCM_ID9359.
Birgit Uytterhoeven   +6 more
doaj   +1 more source

Structural insights into the substrate-bound condensation domains of non-ribosomal peptide synthetase AmbB

open access: yesScientific Reports, 2022
Non-ribosomal peptide synthetases (NRPS) are multi-modular/domain enzymes that catalyze the synthesis of bioactive peptides. A crucial step in the process is peptide elongation accomplished by the condensation (C) domain with the aid of a peptidyl ...
Melissa-Jane Chu Yuan Kee   +7 more
doaj   +1 more source

Adenylation Domain Engineering Enables Biosynthesis of an Improved Polymyxin Antibiotic

open access: yesAngewandte Chemie, Volume 138, Issue 43, 19 October 2026.
To enable incorporation of l‐2‐aminodecanoic acid into polymyxin by fermentation, a single Trp‐to‐Ala substitution is rationally introduced into the adenylation‐domain residue of its nonribosomal peptide synthetase (NRPS) and efficiently switches substrate selectivity. The engineered strain produces biologically active Ada‐polymyxin, demonstrating that
Maximilian Müll   +7 more
wiley   +2 more sources

Peptaibols: Diversity, bioactivity, and biosynthesis

open access: yesEngineering Microbiology, 2022
Peptaibols are a large family of linear, amphipathic polypeptides consisting of 5-20 amino acid residues generated from the fungal nonribosomal peptide synthetase (NRPS) pathway.
Xuewen Hou   +7 more
doaj   +1 more source

Taxonogenomic Analysis of Marine-Derived Streptomyces sp. N11-50 and the Profile of NRPS and PKS Gene Clusters

open access: yesHydrobiology, 2023
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

Biosynthesis of Tetronates by a Nonribosomal Peptide Synthetase–Polyketide Synthase System

open access: yes, 2023
A cryptic tetronate biosynthetic pathway was identified in Kitasatospora niigatensis DSM 44781 via heterologous expression. Distinct from the currently known biosynthetic pathways, this system utilizes a partially functional nonribosomal peptide ...
Wenya Tian (4062244)   +6 more
core   +1 more source

A Fungal Nonribosomal Peptide Synthetase Module that can Synthesize Thiopyrazines

open access: yes, 2016
A nonribosomal peptide synthetase-like enzyme (NRPS325) from Aspergillus terreus was reconstituted in vitro and was shown to synthesize thiopyrazines using an unprecedented mechanism. Substrate promiscuity of NRPS325 toward different amino acids and free
Neil Garg (2216656)   +5 more
core   +1 more source

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