β-Lactone Synthetase Found in the Olefin Biosynthesis Pathway

• DOI: 10.1021/acs.biochem.6b01199
• Publication Date: 2016-12-28T15:26:53Z
• Authors: James K. Christenson; Jack E. Richman; Matthew R. Jensen; Jennifer Y. Neufeld; Carrie M. Wilmot; Lawrence P. Wackett
• Keywords: Biological Products; 0303 health sciences; Sequence Homology, Amino Acid; Stenotrophomonas maltophilia; Gene Expression Regulation, Bacterial; Alkenes; Streptomyces; Lactones; Micrococcus luteus; 03 medical and health sciences; Bacterial Proteins; Multigene Family; Coenzyme A Ligases; Operon; Amino Acid Sequence; Hydroxy Acids

The first β-lactone synthetase enzyme is reported, creating an unexpected link between the biosynthesis of olefinic hydrocarbons and highly functionalized natural products. The enzyme OleC, involved in the microbial biosynthesis of long-chain olefinic hydrocarbons, reacts with syn- and anti-β-hydroxy acid substrates to yield cis- and trans-β-lactones, respectively. Protein sequence comparisons reveal that enzymes homologous to OleC are encoded in natural product gene clusters that generate β-lactone rings, suggesting a common mechanism of biosynthesis.