Pheromone-gland-specific fatty-acyl reductase in the adzuki bean borer, Ostrinia scapulalis (Lepidoptera: Crambidae)

Insect Biochem Mol Biol. 2009 Feb;39(2):90-5. doi: 10.1016/j.ibmb.2008.10.008. Epub 2008 Oct 26.


The adzuki bean borer moth, Ostrinia scapulalis, uses a mixture of (E)-11- and (Z)-11-tetradecenyl acetates as a sex pheromone. At a step in the pheromone biosynthetic pathway, fatty-acyl precursors are converted to corresponding alcohols by an enzyme, fatty-acyl reductase (FAR). Here we report the cloning of FAR-like genes expressed in the pheromone gland of female O. scapulalis, and the characterization of a single pheromone-gland-specific FAR (pgFAR) and its functional assay using an insect cell expression system. As many as thirteen FAR-like genes (FAR-I-FAR-XIII) were expressed in the pheromone gland of O. scapulalis; however, only one (FAR-XIII) was pheromone-gland-specific. The deduced amino acid sequence of FAR-XIII predicted a 462-aa protein with a conserved NAD(P)H-binding motif in the N-terminal region, showing overall identity of 34% with the pgFAR of Bombyx mori. A functional assay using Sf9 cells transfected with an expression vector containing the open reading frame of the FAR-XIII gene has proven that FAR-XIII protein has the ability to convert a natural substrate, (Z)-11-tetradecenoic acid, to a corresponding alcohol, (Z)-11-tetradecenol.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Cloning, Molecular
  • Exocrine Glands / chemistry
  • Exocrine Glands / enzymology
  • Female
  • Insect Proteins / chemistry
  • Insect Proteins / genetics
  • Insect Proteins / metabolism*
  • Molecular Sequence Data
  • Moths / chemistry
  • Moths / enzymology*
  • Moths / genetics
  • Organ Specificity
  • Oxidoreductases / chemistry
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Pheromones / biosynthesis*
  • Sequence Alignment


  • Insect Proteins
  • Pheromones
  • Oxidoreductases