title: Pheromone gland-specific fatty-acyl reductase of the silkmoth, Bombyx mori.
abstract: The C10-C18 unsaturated, acyclic, aliphatic compounds that contain an oxygenated functional group (alcohol, aldehyde, or acetate ester) are a major class of sex pheromones produced by female moths. In the biosynthesis of these pheromone components, the key enzyme required to produce the oxygenated functional groups is fatty-acyl reductase (FAR). This enzyme converts fatty-acyl pheromone precursors to their corresponding alcohols, which, depending on the moth species, can then be acetylated or oxidized to the corresponding aldehydes. Despite the significant role this enzyme has in generating the species-specific oxygenated constituents of lepidopteran sex pheromones, the enzyme has yet to be fully characterized and identified. In experiments designed to characterize a pheromone-gland-specific FAR in the silkmoth, Bombyx mori, we have isolated a cDNA clone encoding a protein homologous to a FAR from the desert shrub, Simmondsia chinensis, commonly known as jojoba. The deduced amino acid sequence of this clone predicts a 460-aa protein with a consensus NAD(P)H binding motif within the amino terminus. Northern blot analysis indicated that 2-kb transcripts of this gene were specifically expressed in the pheromone gland at 1 day before adult eclosion. Functional expression of this gene in the yeast Saccharomyces cerevisiae not only confirmed the long-chain FAR activity, but also indicated a distinct substrate specificity. Finally, the transformed yeast cells evoked typical mating behavior in male moths when cultured with the pheromone precursor fatty acid, (E,Z)-10,12-hexadecadienoic acid.
authors.affiliation: RIKEN, Hirosawa 2-1, Wako, Saitama 351-0198, Japan.
authors.forename: Ken'ichi
authors.initials: K
authors.lastname: Moto
authors.forename: Toyoshi
authors.initials: T
authors.lastname: Yoshiga
authors.forename: Masanobu
authors.initials: M
authors.lastname: Yamamoto
authors.forename: Shunya
authors.initials: S
authors.lastname: Takahashi
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Okano
authors.forename: Tetsu
authors.initials: T
authors.lastname: Ando
authors.forename: Tadashi
authors.initials: T
authors.lastname: Nakata
authors.forename: Shogo
authors.initials: S
authors.lastname: Matsumoto
mesh_terms: D000438:Alcohols / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000737:chemistry*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D012831:Bombyx; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D005260:Female; D008401:Gas Chromatography-Mass Spectrometry; D008297:Male; D008969:Molecular Sequence Data; D010100:Oxygen / Q000378:metabolism; D010675:Pheromones / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012726:Sexual Behavior, Animal; D014018:Tissue Distribution
chemical_list: D000438:Alcohols; D018076:DNA, Complementary; D010675:Pheromones; D010940:Plant Proteins; D000445:Aldehyde Oxidoreductases; C027902:fatty acid reductase; D010100:Oxygen