title: The Yeast ATF1 Acetyltransferase Efficiently Acetylates Insect Pheromone Alcohols: Implications for the Biological Production of Moth Pheromones.
abstract: Many moth pheromones are composed of mixtures of acetates of long-chain (≥10 carbon) fatty alcohols. Moth pheromone precursors such as fatty acids and fatty alcohols can be produced in yeast by the heterologous expression of genes involved in insect pheromone production. Acetyltransferases that subsequently catalyze the formation of acetates by transfer of the acetate unit from acetyl-CoA to a fatty alcohol have been postulated in pheromone biosynthesis. However, so far no fatty alcohol acetyltransferases responsible for the production of straight chain alkyl acetate pheromone components in insects have been identified. In search for a non-insect acetyltransferase alternative, we expressed a plant-derived diacylglycerol acetyltransferase (EaDAcT) (EC 2.3.1.20) cloned from the seed of the burning bush (Euonymus alatus) in a yeast system. EaDAcT transformed various fatty alcohol insect pheromone precursors into acetates but we also found high background acetylation activities. Only one enzyme in yeast was shown to be responsible for the majority of that background activity, the acetyltransferase ATF1 (EC 2.3.1.84). We further investigated the usefulness of ATF1 for the conversion of moth pheromone alcohols into acetates in comparison with Ea DAcT. Overexpression of ATF1 revealed that it was capable of acetylating these fatty alcohols with chain lengths from 10 to 18 carbons with up to 27- and 10-fold higher in vivo and in vitro efficiency, respectively, compared to Ea DAcT. The ATF1 enzyme thus has the potential to serve as the missing enzyme in the reconstruction of the biosynthetic pathway of insect acetate pheromones from precursor fatty acids in yeast.
authors.affiliation: Department of Biology, Lund University, Lund, Sweden. bao-jian.ding@biol.lu.se.
authors.forename: Bao-Jian
authors.initials: BJ
authors.lastname: Ding
authors.affiliation: Department of Plant Breeding, Swedish University of Agricultural Sciences, Alnarp, Sweden.
authors.forename: Ida
authors.initials: I
authors.lastname: Lager
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA.
authors.forename: Sunil
authors.initials: S
authors.lastname: Bansal
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, USA.
authors.forename: Timothy P
authors.initials: TP
authors.lastname: Durrett
authors.affiliation: Department of Plant Breeding, Swedish University of Agricultural Sciences, Alnarp, Sweden.
authors.forename: Sten
authors.initials: S
authors.lastname: Stymne
authors.affiliation: Department of Biology, Lund University, Lund, Sweden.
authors.forename: Christer
authors.initials: C
authors.lastname: Löfstedt
mesh_terms: D000107:Acetylation; D000818:Animals; D005233:Fatty Alcohols / Q000378:metabolism*; D019476:Insect Proteins / Q000378:metabolism; D009036:Moths / Q000737:chemistry*; D010675:Pheromones / Q000096:biosynthesis* / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D005233:Fatty Alcohols; D019476:Insect Proteins; D010675:Pheromones; D011506:Proteins; C079238:alcohol O-acetyltransferase
keywords: Acetates; Acetyltransferase; Fatty alcohol; Moth pheromone; Yeast expression