Abstract
Moth sex pheromone communication has evolved to use complex blends of relatively simple long-chain fatty acid precursors. Species specificity is derived from the unique stereochemistry of double bonds introduced into exact locations along the hydrocarbon backbone of fatty acids, which are reduced and then undergo a variety of chain-shortening and functionalization reactions to form the pheromone blend. Key enzymes that have evolved to function in this system are the acyl coenzyme A desaturases, which catalyze the introduction of the double bonds. This report gives an overview of the evolution of these enzymes, with an introduction to the newly arisen field of "semiochemical genetics."
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