Titlebook: Nonribosomal Peptide and Polyketide Biosynthesis; Methods and Protocol Bradley S. Evans Book 2016 Springer Science+Business Media New York

Inexorable

Colorimetric Detection of the Adenylation Activity in Nonribosomal Peptide Synthetasesomains determine the amino-acid building blocks to be incorporated during nonribosomal peptide biosynthesis. The A-domains mediate ATP-dependent activation of amino-acid substrates as aminoacyl-.-AMP with pyrophosphate (PPi) release. Traditionally, the enzymatic activity of the A-domains has been me

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Facile Synthetic Access to Glycopeptide Antibiotic Precursor Peptides for the Investigation of Cytocds all stems from in vivo biosynthesis, understanding the mechanisms of the natural assembly system—consisting of a nonribosomal-peptide synthetase machinery (NRPS) and further modifying enzymes—is vital. In order to address the later steps of peptide biosynthesis, which are catalyzed by Cytochrome

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Reconstitution of Fungal Nonribosomal Peptide Synthetases in Yeast and In VitroNRPSs). However, there remain challenges for the characterization of these megasynthases. While genetic methods in native hosts are critical in elucidation of the function of fungal NRPS, in vitro assays of intact heterologously expressed proteins provide deeper mechanistic insights in NRPS enzymolo

Ergots

The Continuing Development of , as a Heterologous Host for Complex Natural Product Biosynthesisn motivated by limitations inherent in native production hosts, the heterologous biosynthetic process begins with a candidate host regarded as technically advanced relative to original producing organisms. Given this requirement, . has been a top choice for heterologous biosynthesis attempts as asso

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Screening for Expressed Nonribosomal Peptide Synthetases and Polyketide Synthases Using LC-MS/MS-Basroughput fashion. Herein we report a protocol using LC-MS/MS-based proteomics for the screening of enzymes involved in natural product biosynthesis, such as nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs) from bacterial strains. Taking advantage of the large size of modular

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In Situ Analysis of Bacterial Lipopeptide Antibiotics by Matrix-Assisted Laser Desorption/Ionizationnal mapping of a broad variety of biomolecules present at the surface of a sample. In many applications including pharmaceutical studies or biomarker discovery, the distribution of proteins, lipids or drugs, and metabolites may be visualized within tissue sections. More recently, MALDI MSI has becom

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