6533b860fe1ef96bd12c3945
RESEARCH PRODUCT
Degradation of an alkaloid pheromone from the pale-brown chafer, Phyllopertha diversa (Coleoptera: Scarabaeidae), by an insect olfactory cytochrome P450.
Walter S. LealHubert WojtasekWalter Leal Filhosubject
pheromone-degrading enzymemedia_common.quotation_subjectBiophysicsInsectOlfactionscarab beetleBiochemistryMass SpectrometryHydroxylationchemistry.chemical_compoundAlkaloidsCytochrome P-450 Enzyme SystemStructural BiologyMicrosomesBotanyGeneticsAnimalsCytochrome P-450 Enzyme InhibitorsEnzyme InhibitorsSex AttractantsMolecular BiologyChromatography High Pressure LiquidDemethylationmedia_commonbiologyMolecular StructureProadifenCytochrome P450Cell BiologyMetyraponeProadifenColeopteraBiochemistrychemistrySex pheromonebiology.proteinQuinazolinesPheromoneInsect ProteinsChromatography Thin Layerpheromone inactivationolfactiondescription
AbstractThe pale-brown chafer, Phyllopertha diversa, utilizes an unusual alkaloid, 1,3-dimethyl-2,4-(1H,3H)-quinazolinedione, as its sex pheromone. This compound is rapidly degraded in vitro by the antennal protein extracts from this scarab beetle. Demethylation at the N-1 position and hydroxylation of the aromatic ring have been identified as the major catabolic pathways. The enzyme responsible for the pheromone degradation is membrane-bound, requires NAD(P)H for activity and is sensitive to cytochrome P450 inhibitors, such as proadifen and metyrapone. The ability to metabolize this unusual pheromone was not detected in 12 species tested, indicating that the P450 system, specific to male P. diversa antennae, has evolved as a mechanism for olfactory signal inactivation.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-09-21 | FEBS letters |