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Extending Polyketide Structural Diversity by Using Engineered Carboxylase/Reductase Enzymes
Author(s) -
Kundert Jana,
Gulder Tobias A. M.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201510402
Subject(s) - polyketide , carboxylation , pyruvate carboxylase , chemistry , stereochemistry , enzyme , biochemistry , polyketide synthase , active site , reductase , diversification (marketing strategy) , biosynthesis , catalysis , marketing , business
For a change : Enoyl‐CoA carboxylase/reductases (ECRs) catalyze the selective α‐carboxylation of α,β‐unsaturated CoA‐thioesters. Structure‐based engineering of the active‐site binding pocket of ECRs enabled significant alteration of their catalytic activity towards larger substrates. This facilitates the incorporation of unusual extender units into polyketide backbones, thus providing a novel method for the directed structural diversification of polyketides.