Journal
FEBS LETTERS
Volume 594, Issue 7, Pages 1187-1195Publisher
WILEY
DOI: 10.1002/1873-3468.13718
Keywords
Drosophila GSTE14; ecdysteroid; glutathione transferase; Noppera-bo; steroid double-bond isomerization
Funding
- Swedish Research Council [2015-04222, 2018-03406]
- Agence Nationale de la Recherche [ANR-16-CE21-0004-01]
- Swedish Cancer Society
- ERDF/ESF, OP RDE, project IOCB Mobility [CZ.02.2.69/0.0/0.0/16_027/0008477]
- Agence Nationale de la Recherche (ANR) [ANR-16-CE21-0004] Funding Source: Agence Nationale de la Recherche (ANR)
- Swedish Research Council [2015-04222] Funding Source: Swedish Research Council
- Vinnova [2015-04222] Funding Source: Vinnova
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Ecdysteroids are critically important for the formation of the insect exoskeleton. Cholesterol is a precursor of ecdysone and its active form 20-hydroxyecdysone, but some steps in the ecdysteroid biosynthesis pathway remain unknown. An essential requirement of glutathione (GSH) transferase GSTE14 in ecdysteroid biosynthesis has been established in Drosophila melanogaster, but its function is entirely unknown. Here, we have determined the crystal structure of GSTE14 in complex with GSH and investigated the kinetic properties of GSTE14 with alternative substrates. GSTE14 has high-ranking steroid double-bond isomerase activity, albeit 50-fold lower than the most efficient mammalian GSTs. Corresponding steroid isomerizations are unknown in insects, and their exact physiological role remains to be shown. Nonetheless, the essential enzyme GSTE14 is here demonstrated to be catalytically competent and have a steroid-binding site.
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