Data in support of substrate flexibility of a mutated acyltransferase domain and implications for polyketide biosynthesis

Enzyme-directed mutasynthesis is an emerging strategy for the targeted derivatization of natural products. Here, data on the synthesis of malonic acid derivatives for feeding studies in Saccharopolyspora erythraea , the mutagenesis of DEBS and bioanalytical data on the experimental investigation of...

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Published in:Data in brief Vol. 5; no. C; pp. 528 - 536
Main Authors: Klopries, Stephan, Bravo-Rodriguez, Kenny, Koopmans, Kyra R.M., Sundermann, Uschi, Yahiaoui, Samir, Arens, Julia, Kushnir, Susanna, Sanchez-Garcia, Elsa, Schulz, Frank
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Abstract Enzyme-directed mutasynthesis is an emerging strategy for the targeted derivatization of natural products. Here, data on the synthesis of malonic acid derivatives for feeding studies in Saccharopolyspora erythraea , the mutagenesis of DEBS and bioanalytical data on the experimental investigation of studies on the biosynthetic pathway towards erythromycin are presented.
AbstractList Enzyme-directed mutasynthesis is an emerging strategy for the targeted derivatization of natural products. Here, data on the synthesis of malonic acid derivatives for feeding studies in Saccharopolyspora erythraea , the mutagenesis of DEBS and bioanalytical data on the experimental investigation of studies on the biosynthetic pathway towards erythromycin are presented.
Enzyme-directed mutasynthesis is an emerging strategy for the targeted derivatization of natural products. Here, data on the synthesis of malonic acid derivatives for feeding studies in Saccharopolyspora erythraea , the mutagenesis of DEBS and bioanalytical data on the experimental investigation of studies on the biosynthetic pathway towards erythromycin are presented.
Author Schulz, Frank
Sanchez-Garcia, Elsa
Klopries, Stephan
Bravo-Rodriguez, Kenny
Kushnir, Susanna
Sundermann, Uschi
Arens, Julia
Koopmans, Kyra R.M.
Yahiaoui, Samir
AuthorAffiliation d Université de Caen Basse-Normandie, Centre d’Etudes et de Recherche sur le Médicament de Normandie, F-14032 Caen, France
a Fakultät für Chemie und Biochemie, Organische Chemie 1, Ruhr-Universität Bochum, Universitätsstraße 150, 44780 Bochum, Germany
c Dr. Fooke-Achterrath Laboratorien GmbH, Habichtweg 16, 41468 Neuss, Germany
b Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany
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Cites_doi 10.1002/cbic.201100383
10.1016/j.chembiol.2015.02.008
10.1002/anie.201202438
10.1021/cb300505w
10.1021/jo00908a030
10.1016/S0040-4039(01)99819-3
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Title Data in support of substrate flexibility of a mutated acyltransferase domain and implications for polyketide biosynthesis
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