title: β-Lactone Synthetase Found in the Olefin Biosynthesis Pathway.
abstract: 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.
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota , Minneapolis, Minnesota 55455, United States.|BioTechnology Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.
authors.forename: James K
authors.identifier: http://orcid.org/0000-0002-2597-9951
authors.initials: JK
authors.lastname: Christenson
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota , Minneapolis, Minnesota 55455, United States.|BioTechnology Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.
authors.forename: Jack E
authors.initials: JE
authors.lastname: Richman
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota , Minneapolis, Minnesota 55455, United States.|BioTechnology Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Jensen
authors.affiliation: BioTechnology Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.
authors.forename: Jennifer Y
authors.initials: JY
authors.lastname: Neufeld
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota , Minneapolis, Minnesota 55455, United States.|BioTechnology Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.
authors.forename: Carrie M
authors.initials: CM
authors.lastname: Wilmot
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota , Minneapolis, Minnesota 55455, United States.|BioTechnology Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.|Microbial and Plant Genomic Institute, University of Minnesota , St. Paul, Minnesota 55108, United States.
authors.forename: Lawrence P
authors.initials: LP
authors.lastname: Wackett
mesh_terms: D000475:Alkenes / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001688:Biological Products / Q000378:metabolism; D003066:Coenzyme A Ligases / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006880:Hydroxy Acids; D007783:Lactones / Q000378:metabolism*; D016982:Micrococcus luteus / Q000201:enzymology / Q000235:genetics*; D005810:Multigene Family; D009876:Operon; D017386:Sequence Homology, Amino Acid; D020615:Stenotrophomonas maltophilia / Q000201:enzymology / Q000235:genetics*; D013302:Streptomyces / Q000201:enzymology / Q000235:genetics*
chemical_list: D000475:Alkenes; D001426:Bacterial Proteins; D001688:Biological Products; D006880:Hydroxy Acids; D007783:Lactones; D003066:Coenzyme A Ligases