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Functional analyses were performed with microsomal human 11beta-hydroxysteroid dehydrogenase type 1 overexpressed in the yeast Pichia pastoris. Cell extracts or microsomes from transformed strains displayed dehydrogenase and reductase activities, which were up to 10 times higher than in human liver microsomes, while for whole cells cortisone reduction but no dehydrogenase activity was observed. The synthetic glucocorticoids prednisolone and prednisone were efficiently metabolized by subcellular fractions, whereas no activity was observed with dexamethasone, budesonide and deflazacort. Inhibitors found to be effective towards the recombinant 11beta-hydroxysteroid dehydrogenase include synthetic steroids and xenobiotic compounds, revealing selective inhibition of the reaction direction, useful for development of specific inhibitors.

Original publication




Journal article


Febs lett

Publication Date





25 - 28


11-beta-Hydroxysteroid Dehydrogenases, Cloning, Molecular, Enzyme Inhibitors, Estradiol Congeners, Flavanones, Flavonoids, Furosemide, Humans, Hydroxysteroid Dehydrogenases, Kinetics, Microsomes, Pichia, Recombinant Proteins, Steroids, Substrate Specificity, Xenobiotics