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

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

doi:10.1016/j.dib.2015.09.052

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

Data Brief. 2015 Oct 14:5:528-36. doi: 10.1016/j.dib.2015.09.052. eCollection 2015 Dec.

Authors

Stephan Klopries¹, Kenny Bravo-Rodriguez², Kyra R M Koopmans¹, Uschi Sundermann³, Samir Yahiaoui⁴, Julia Arens¹, Susanna Kushnir¹, Elsa Sanchez-Garcia², Frank Schulz¹

Affiliations

¹ Fakultät für Chemie und Biochemie, Organische Chemie 1, Ruhr-Universität Bochum, Universitätsstraße 150, 44780 Bochum, Germany.
² Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.
³ Dr. Fooke-Achterrath Laboratorien GmbH, Habichtweg 16, 41468 Neuss, Germany.
⁴ Université de Caen Basse-Normandie, Centre d'Etudes et de Recherche sur le Médicament de Normandie, F-14032 Caen, France.

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.