The enzyme acts on multiple 3beta-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17beta-estradiol 17-dehydrogenase .
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SYSTEMATIC NAME
IUBMB Comments
3beta-hydroxysteroid:NADP+ 3-oxidoreductase
The enzyme acts on multiple 3beta-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17beta-estradiol 17-dehydrogenase [4].
in NS0 cells deficient in 17beta-hydroxysteroid dehydrogenase type 7 activity, oxidosqualene cyclase is fully active. The protective role of the 3-ketoreductase in yeasts with respect to oxidosqualene cyclase activity is not conserved in mammals
expression of mouse mouse 3-keto-steroid reductase Erg27 in a Saccharomyces cerevisiae Erg27 mutant confers the ability to grow using lanosterol as a substrate. The mouse orthologue complements the erg27 lesion but is unable to restore Erg7, i.e. lanosterol synthase, activity. The recombinant strain accumulates squalene epoxides, 3-ketosterones, and ergosterol
overexpression of 17beta-hydroxysteroid dehydrogenase type 7 in ERG27-deleted yeast cells. Recombinant strains grow more slowly than the control yeast ERG27-overexpressing strain on sterol-deficient media, whereas the growth rate is normal on media supplemented with a 3-ketoreductase substrate. Mammalian steroid-3-ketoreductase expressed in yeast shows full enzymatic functioanlity but is unable to support the functionality of yeast oxidosqualene cyclase as ERG27 does
overexpression of 17beta-hydroxysteroid dehydrogenase type 7 in ERG27-deleted yeast cells. Recombinant strains grow more slowly than the control yeast ERG27-overexpressing strain on sterol-deficient media, whereas the growth rate is normal on media supplemented with a 3-ketoreductase substrate. Mammalian steroid-3-ketoreductase expressed in yeast shows full enzymatic functioanlity but is unable to support the functionality of yeast oxidosqualene cyclase as ERG27 does
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of HSD17B7 as a glutathione-S-transferase fusion protein in Escherichia coli. Erg27p-deficient yeast strain complements the 3-ketosteroid reductase deficiency of the cells and restores growth on sterol-deficient medium
Characterization of a mutation that results in independence of oxidosqualene cyclase (Erg7) activity from the downstream 3-ketoreductase (Erg27) in the yeast ergosterol biosynthetic pathway