Journal
BIOMOLECULES
Volume 13, Issue 6, Pages -Publisher
MDPI
DOI: 10.3390/biom13060976
Keywords
Nobo; Anopheles gambiae GSTE8; malaria; ketosteroids; ecdysteroidogenesis
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Nobo is a crucial glutathione transferase (GST) in insects that contributes to their growth and the spread of diseases. It has been found to have efficient hydroxylase activity in insects containing the ketosteroid. Specific amino acid residues are essential for the catalytic activity of Nobo.
Nobo is a glutathione transferase (GST) crucially contributing to ecdysteroid biosynthesis in insects of the orders Diptera and Lepidoptera. Ecdysone is a vital steroid hormone in insects, which governs larval molting and metamorphosis, and the suppression of its synthesis has potential as a novel approach to insect growth regulation and combatting vectors of disease. In general, GSTs catalyze detoxication, whereas the specific function of Nobo in ecdysteroidogenesis is unknown. We report that Nobo from the malaria-spreading mosquito Anopheles gambiae is a highly efficient ketosteroid isomerase catalyzing double-bond isomerization in the steroids 5-androsten-3,17-dione and 5-pregnen-3,20-dione. These mammalian ketosteroids are unknown in mosquitoes, but the discovered prominent catalytic activity of these compounds suggests that the unknown Nobo substrate in insects has a ketosteroid functionality. Aminoacid residue Asp111 in Nobo is essential for activity with the steroids, but not for conventional GST substrates. Further characterization of Nobo may guide the development of new insecticides to prevent malaria.
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