Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity.

Journal article

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, prostaglandins and xenobiotics. In vitro, DHRS10 converts...

Expand abstract

Authors: Lukacik, P; Keller, B; Bunkoczi, G; Kavanagh, K; Kavanagh, K

• Publication status: Published
• Journal: Biochemical journal
• Volume: 402
• Issue: 3
• Pages: 419-427
• Publication date: 2007-03-01
• DOI: 10.1042/bj20061319
• EISSN: 1470-8728
• ISSN: 0264-6021
• Language: English
• Keywords: Ligands; Amino Acid Sequence; 17-Hydroxysteroid Dehydrogenases; Models, Molecular; Oxidation-Reduction; Cytosol; Organ Specificity; Humans; Gene Expression; Crystallography, X-Ray; Cell Line; Protein Structure, Secondary; Sequence Alignment; Kinetics; Structural Homology, Protein; Binding Sites; Molecular Sequence Data; NAD; Protein Structure, Tertiary