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The human enzyme 11beta-hydroxysteroid dehydrogenase (11beta-HSD) catalyzes the reversible oxidoreduction of 11beta-OH/11-oxo groups of glucocorticoid hormones. Besides this important endocrinological property, the type 1 isozyme (11beta-HSD1) mediates reductive phase I reactions of several carbonyl group bearing xenobiotics, including drugs, insecticides and carcinogens. The aim of this study was to explore novel substrate specificities of human 11beta-HSD1, using heterologously expressed protein in the yeast system Pichia pastoris. In addition to established phase I xenobiotic substrates, it is now demonstrated that transformed yeast strains catalyze the reduction of ketoprofen to its hydroxy metabolite, and the oxidation of the prodrug DFU-lactol to the pharmacologically active lactone compound. Purified recombinant 11beta-HSD1 mediated oxidative reactions, however, the labile reductive activity component could not be maintained. In conclusion, evidence is provided that human 11beta-HSD1 in vitro is involved in phase I reactions of anti-inflammatory non-steroidal drugs like ketoprofen and DFU-lactol.

Original publication




Journal article


Chem biol interact

Publication Date





805 - 814


11-beta-Hydroxysteroid Dehydrogenase Type 2, Anti-Inflammatory Agents, Non-Steroidal, Cyclooxygenase Inhibitors, Gene Expression, Humans, Hydroxysteroid Dehydrogenases, In Vitro Techniques, Ketoprofen, Oxidation-Reduction, Pichia, Prodrugs, Recombinant Proteins, Substrate Specificity, Xenobiotics