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Title

Identification and characterization of a fatty acyl reductase from a Spodoptera littoralis female gland involved in pheromone biosynthesis

AuthorsCarot-Sans, Gerard CSIC ORCID; Muñoz, Lourdes CSIC ORCID; Piulachs, Maria-Dolors CSIC ORCID ; Guerrero, Ángel CSIC ORCID; Rosell, Gloria CSIC ORCID
KeywordsFatty acyl-CoA reductase
Spodoptera littoralis
cDNA identification
Pheromone biosynthesis
Enzyme kinetics
Egyptian cotton leaf worm
Issue DateFeb-2015
PublisherJohn Wiley & Sons
CitationInsect Molecular Biology 24(1): 82-92 (2015)
Abstract© 2014 Royal Entomological Society. Fatty acyl-CoA reductases (FARs), the enzymes that catalyse reduction of a fatty acyl-CoA to the corresponding alcohol in insect pheromone biosynthesis, are postulated to play an important role in determining the proportion of each component in the pheromone blend. For the first time, we have isolated and characterized from the Egyptian cotton leaf worm Spodoptera littoralis (Lepidoptera: Noctuidae) a FAR cDNA (Slit-FAR1), which appeared to be expressed only in the pheromone gland and was undetectable in other female tissues, such as fat body, ovaries, wings, legs or thorax. The encoded protein has been successfully expressed in a recombinant system, and the recombinant enzyme is able to produce the intermediate fatty acid alcohols of the pheromone biosynthesis of S. littoralis from the corresponding acyl-CoA precursors. The kinetic variables Km and Vmax, which have been calculated for each acyl-CoA pheromone precursor, suggest that in S. littoralis pheromone biosynthesis other biosynthetic enzymes (e.g. desaturases, acetyl transferase) should also contribute to the final ratio of components of the pheromone blend. In a phylogenetic analysis, Slit-FAR1 appeared grouped in a cluster of other FARs involved in the pheromone biosynthesis of other insects, with little or non-specificity for the natural pheromone precursors.
Publisher version (URL)http://dx.doi.org/10.1111/imb.12138
URIhttp://hdl.handle.net/10261/113028
DOIhttp://dx.doi.org/10.1111/imb.12138
Identifiersdoi: 10.1111/imb.12138
e-issn: 1365-2583
issn: 0962-1075
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