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Characterization of oxidase(s) associated with the sex pheromone gland in <i>Manduca sexta</i> (L.) females
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Citations
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References
1995
Year
Primary Aliphatic AlcoholsGeneticsFemale Reproductive FunctionReproductive BiologyUnited StatesRedox BiologyBiosynthesisPublic HealthAlcohol DehydrogenasesPheromone BiochemistryAldehyde DehydrogenaseBiochemistrySemiochemicalEndocrinologySex Pheromone GlandU.s. Government WorkBiologyMetabolismMedicine
Abstract An oxidase that converts primary aliphatic alcohols into aldehydes was discovered in the cuticle of the sex pheromone gland and in the papillae anales on the tip of the abdomen of Manduca sexta females. Oxidase activity was not found in the epidermal cells of the pheromone gland where fatty acid precursors of the pheromonal aldehydes are found. This oxidase requires oxygen and water to function and appears to have a rather broad substrate specificity. The activity of the oxidase is reduced by the application of piperonyl butoxide, which also interferes with the PBAN induced production of the natural pheromone aldehydes. However, endogenous alcohols cannot be found in the pheromone gland. Thus, it is not yet clear whether or not the oxidase is involved in the terminal step of biosynthesis of the pheromone aldehydes in M. sexta females. © Wiley‐Liss, Inc. This article is a U.S. Government work and, a such, is in the public domain in the United States of America.
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