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Functional characterization of fatty acyl-CoA reductases from Drosophila melanogaster
AuthorWickenberg, Leah Plaugher
Biochemistry and Molecular Biology
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Fossil fuels are a finite resource, making research into alternative energy sources a high priority. Biological hydrocarbon production may contribute to technologies that replace fossil fuels. Hydrocarbon production from fatty acyl-CoA precursors in insects proceeds through a reduction of fatty acyl-CoA to an aldehyde, followed by aldehyde decarbonylation to yield hydrocarbon. This study focused on the reduction mechanism, catalyzed by a fatty acyl-CoA reductase (FAR) through efforts to functionally characterize three FAR enzymes from Drosophila melanogaster: CG18031, CG13091 and CG17562. All three FARs were heterologously produced in Sf9 cells using a baculoviral expression system and assayed with a variety of substrates. CG18031 converted 26 acyl-CoA to C26 alcohol and appears to prefer long-chain substrates. No activity was found when CG18031 was assayed with shorter chain (C24 or C24:1) substrates. No activity was observed with any substrate when CG17562 or CG13091 were assayed. These data suggest that insect FARs have narrow substrate ranges, and additional assays must be performed in order to identify an aldehyde producing FAR.