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

Klopries, Stephan; Bravo-Rodriguez, Kenny; Koopmans, Kyra R. M.; Sundermann, Uschi; Yahiaoui, Samir; Arens, Julia; Kushnir, Susanna; Sanchez Garcia, Elsa; Schulz, Frank

doi:10.1016/j.dib.2015.09.052

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

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Bravo-Rodriguez, Kenny
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Sanchez Garcia, Elsa
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Klopries, S., Bravo-Rodriguez, K., Koopmans, K. R. M., Sundermann, U., Yahiaoui, S., Arens, J., et al. (2015). Data in support of substrate flexibility of a mutated acyltransferase domain and implications for polyketide biosynthesis. Data in Brief, 5, 528-536. doi:10.1016/j.dib.2015.09.052.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-644A-8

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.