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Biochem Biophys Res Commun ; 711: 149914, 2024 Jun 04.
Artículo en Inglés | MEDLINE | ID: mdl-38608434

RESUMEN

The steroid hormone ecdysone is essential for the reproduction and survival of insects. The hormone is synthesized from dietary sterols such as cholesterol, yielding ecdysone in a series of consecutive enzymatic reactions. In the insect orders Lepidoptera and Diptera a glutathione transferase called Noppera-bo (Nobo) plays an essential, but biochemically uncharacterized, role in ecdysteroid biosynthesis. The Nobo enzyme is consequently a possible target in harmful dipterans, such as disease-carrying mosquitoes. Flavonoid compounds inhibit Nobo and have larvicidal effects in the yellow-fever transmitting mosquito Aedes aegypti, but the enzyme is functionally incompletely characterized. We here report that within a set of glutathione transferase substrates the double-bond isomerase activity with 5-androsten-3,17-dione stands out with an extraordinary specific activity of 4000 µmol min-1 mg-1. We suggest that the authentic function of Nobo is catalysis of a chemically analogous ketosteroid isomerization in ecdysone biosynthesis.


Asunto(s)
Aedes , Aedes/enzimología , Aedes/metabolismo , Animales , Glutatión Transferasa/metabolismo , Glutatión/metabolismo , Ecdisona/metabolismo , Proteínas de Insectos/metabolismo , Especificidad por Sustrato , Esteroide Isomerasas/metabolismo , Esteroide Isomerasas/genética , Mosquitos Vectores/metabolismo , Cetosteroides/metabolismo , Cetosteroides/química
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