Results 111 to 120 of about 10,782 (215)

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

Exploring the Domain Structure of Modular Nonribosomal Peptide Synthetases

open access: yes, 2001
Recently, considerable insight has been gained into the modular organization of nonribosomal peptide synthetases (NRPS). The three-dimensional structures of domains associated with substrate adenylation and covalent binding have been solved as well as ...
Marahiel, Mohamed A   +3 more
core   +1 more source

The cycloaspeptides:uncovering a new model for methylated nonribosomal peptide biosynthesis [PDF]

open access: yes, 2018
The cycloaspeptides are bioactive pentapeptides produced by various filamentous fungi, which have garnered interest from the agricultural industry due to the reported insecticidal activity of the minor metabolite, cycloaspeptide E.
Simpson, Tom   +28 more
core   +1 more source

Mechanistic Insights Into the Biosynthesis of Pseurotin A in Aspergillus fumigatus

open access: yesSmall Structures
The biosynthesis of pseurotin A, a fungal metabolite with antibiotic and immunosuppressive properties, involves a group of enzymes, including a polyketide‐nonribosomal peptide synthase (PKS‐NRPS), PsoA, and a bifunctional enzyme, PsoF. PsoA consists of a
Lei Sun   +5 more
doaj   +1 more source

Cell-free protein synthesis for nonribosomal peptide synthetic biology

open access: yesFrontiers in Natural Products
Peptide natural products have a wide range of useful applications as pesticides, veterinary agents, pharmaceuticals, and bioproducts. To discover new natural products, manipulate them for analog generation, and to harness the potential of these bioactive
Tien T. Sword   +2 more
doaj   +1 more source

Desymmetrization of Cyclodepsipeptides by Assembly Mode Switching of Iterative Nonribosomal Peptide Synthetases

open access: yes, 2019
Nonribosomal peptide synthetases assemble a considerable number of structurally complex peptides of pharmacological importance. This turns them into important biosynthetic machineries for peptide diversification by engineering approaches.
Sylvester Hoffmann (6481823)   +5 more
core   +1 more source

ANTI-BACTERIAL PROPERTY OF A CORAL-ASSOCIATED BACTERIUM Bacillus sp. AGAINST CORAL PATHOGENIC [PDF]

open access: yes, 2006
Marine organisms such as corals are frequently colonized by bacteria that may be pathogenic to them. One of the means by which they are able to combat microbial attack is by chemical defense.
Radjasa, Ocky Karna, Sabdono, Agus
core  

Recent advances in engineering nonribosomal peptide assembly lines.

open access: yes, 2016
Covering: up to July 2015Nonribosomal peptides are amongst the most widespread and structurally diverse secondary metabolites in nature with many possessing bioactivity that can be exploited for therapeutic applications.
Winn, Michael   +3 more
core   +1 more source

Interdomain and Intermodule Organization in Epimerization Domain Containing Nonribosomal Peptide Synthetases

open access: yes, 2016
Nonribosomal peptide synthetases are large, complex multidomain enzymes responsible for the biosynthesis of a wide range of peptidic natural products. Inherent to synthetase chemistry is the thioester templated mechanism that relies on protein/protein ...
Naga Sandhya Guntaka (2852846)   +3 more
core   +1 more source

Expanding the Chemical Space of Nonribosomal Peptide Synthetase-like Enzymes by Domain and Tailoring Enzyme Recombination

open access: yes, 2018
The potential of tailoring enzymes in combination with engineered hybrid nonribosomal peptide synthetase-like enzymes was explored and resulted in methylated and prenylated forms of novel natural products, highlighting the possibilities and limitations ...
Clay C. C. Wang   +3 more
core   +1 more source

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