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- Title
An Unusual Dehydratase Acting on Glycerate and a Ketoreducatse Stereoselectively Reducing α-Ketone in Polyketide Starter Unit Biosynthesis.
- Authors
He, Hai ‐ Yan; Yuan, Hua; Tang, Man ‐ Cheng; Tang, Gong ‐ Li
- Abstract
Polyketide synthases (PKSs) usually employ a ketoreductase (KR) to catalyze the reduction of a β-keto group, followed by a dehydratase (DH) that drives the dehydration to form a double bond between the α- and β-carbon atoms. Herein, a DH*-KR* involved in FR901464 biosynthesis was characterized: DH* acts on glyceryl-S-acyl carrier protein (ACP) to yield ACP-linked pyruvate; subsequently KR* reduces α-ketone that yields L-lactyl-S-ACP as starter unit for polyketide biosynthesis. Genetic and biochemical evidence was found to support a similar pathway that is involved in the biosynthesis of lankacidins. These results not only identified new PKS domains acting on different substrates, but also provided additional options for engineering the PKS starter pathway or biocatalysis.
- Subjects
POLYKETIDE synthases; BIOSYNTHESIS; STEREOSELECTIVE reactions; DOUBLE bonds; REDUCTION of ketones; ACYL carrier protein
- Publication
Angewandte Chemie, 2014, Vol 126, Issue 42, p11497
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201406602