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

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Alignment-Free Methods for the Detection and Specificity Prediction of Adenylation Domainsrs), which in a first step uses protein four-color maps to represent A-domains. In a second step, simple topological indices (TIs), called spectral moments, are derived from the graphical representations of known A-domains (positive dataset) and of unrelated but well-characterized sequences (negativ

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1064-3745 rence for those experienced in studying NRPS and PKS enzymes, pathways, and natural products as well as a gateway for those just entering the field..978-1-4939-8034-5978-1-4939-3375-4Series ISSN 1064-3745 Series E-ISSN 1940-6029

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The Assembly Line Enzymology of Polyketide Biosynthesis, agrochemicals, and veterinary medicines. In bacteria complex polyketides are biosynthesized by giant multifunctional megaenzymes, termed modular polyketide synthases (PKSs), which construct their products in a highly coordinated assembly line-like fashion from a pool of simple precursor substrates

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Measurement of Nonribosomal Peptide Synthetase Adenylation Domain Activity Using a Continuous Hydrox are considered the gatekeepers of NRPSs since they select, activate, and load the carboxylic acid substrate onto a downstream peptidyl carrier protein (PCP) domain of the NRPS. We describe a coupled continuous kinetic assay for NRPS adenylation domains that substitutes the PCP domain with hydroxyla

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Affinity Purification Method for the Identification of Nonribosomal Peptide Biosynthetic Enzymes Usi adenylation (A) domains in nonribosomal peptide synthetases (NRPSs). We recently developed an affinity probe for A domains that could be used to facilitate the specific isolation and identification of NRPS modules. Our synthetic probe, which is a biotinylated variant of .-Phe-AMS (.-Phe-AMS-biotin)