Structure and function of human 17beta-hydroxysteroid dehydrogenases.
|Abstract||17Beta-hydroxysteroid dehydrogenases (17beta-HSDs) catalyze the NAD(P)(H) dependent oxidoreduction at C17 oxo/beta-hydroxyl groups of androgen and estrogen hormones. This reversible reaction constitutes an important pre-receptor control mechanism for nuclear receptor ligands, since the conversion "switches" between the 17beta-OH receptor ligands and their inactive 17-oxo metabolites. At present, 14 mammalian 17beta-HSDs are described, of which at ... [truncated at 450 characters in length]|
|Author||Lukacik, Petra; Kavanagh, Kathryn L; Oppermann, Udo;|
|Subject||17-Hydroxysteroid Dehydrogenases Humans Protein Conformation Substrate Specificity chemistry drug effects physiology|
Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity.
|Abstract||To this day, a significant proportion of the human genome remains devoid of functional characterization. In this study, we present evidence that the previously functionally uncharacterized product of the human DHRS10 gene is endowed with 17beta-HSD (17beta-hydroxysteroid dehydrogenase) activity. 17beta-HSD enzymes are primarily involved in the metabolism of steroids at the C-17 position and also of other substrates such as fatty acids, prostaglan ... [truncated at 450 characters in length]|
|Author||Lukacik, Petra; Keller, Brigitte; Bunkoczi, Gabor; et al|
|Subject||17-Hydroxysteroid Dehydrogenases Amino Acid Sequence Binding Sites Cell Line Crystallography, X-Ray Cytosol Gene Expression Humans Kinetics Ligands Models, Molecular Molecular Sequence Data NAD Organ Specificity Oxidation-Reduction Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Structural Homology, Protein chemistry genetics isolation and purification metabolism enzymology metabolism|