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

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

doi:10.1016/j.dib.2015.09.052

Stephan Klopries, Elsa Sanchez-Garcia + Show 7 more

Open Access

https://doi.org/10.1016/j.dib.2015.09.052

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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.

Highlights

Enzyme-directed mutasynthesis is an emerging strategy for the targeted derivatization of natural products
Analyzed Synthesis products were analyzed after chromatographic purification, biosynthesis products were solid-phase extracted from fermentation broth Analogues of biosynthetic building blocks were chemically synthesized and supplied to mutated strains of S. erythraea
The data shown here substantiate the exploration of the mutated polyketide synthase which directs the biosynthesis of erythryomcin in Saccharopolyspora erythraea

Summary

Data accessibility

Analyzed Synthesis products were analyzed after chromatographic purification, biosynthesis products were solid-phase extracted from fermentation broth Analogues of biosynthetic building blocks were chemically synthesized and supplied to mutated strains of S. erythraea. Data on the site-directed mutagenesis of 6-deoxyerythronolide B synthase (DEBS) in S. erythraea are presented. The data shown here substantiate the exploration of the mutated polyketide synthase which directs the biosynthesis of erythryomcin in Saccharopolyspora erythraea. Biomolecular modeling was able to further the design and implementation of additional mutations in the active site of DEBS AT6, which decrease the steric constraints and improve the incorporation of the synthetic substrate 2 into the resulting polyketide. The synthesis of artificial extender unit analogs for polyketide biosynthesis and the mutagenesis of an acyltransferase domain for acceptance of these building blocks are described. The data on feeding experiments in S. erythraea are shown

General information

Findings

Synthesis of compounds 1–7