Initial characterization of human DHRS1 (SDR19C1), a member of the short-chain dehydrogenase/reductase superfamily
| Autor: | Lucie Zemanová, Vladimír Wsól, Jerzy Adamski, Marc Meier, Miroslav Šafr, Kristýna Šperková, Eva Novotná, Jiří Andrejs, Rudolf Andrýs, Gabriele Möller, Klára Kozáková, Hana Navrátilová |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Carbonyl Reductase Estrone Endocrinology Diabetes and Metabolism In silico Clinical Biochemistry Dehydrogenase Reductase Endoplasmic Reticulum Biochemistry DHRS1 Short Chain Dehydrogenase-Reductases 03 medical and health sciences 0302 clinical medicine Endocrinology Cell Line Tumor Adrenal Glands Sf9 Cells Animals Humans Amino Acid Sequence Molecular Biology chemistry.chemical_classification Short-chain dehydrogenase Endoplasmic reticulum Cell Biology Recombinant Proteins Cortisone 030104 developmental biology Enzyme Liver chemistry 030220 oncology & carcinogenesis Molecular Medicine Oxidoreductases HeLa Cells |
| Zdroj: | The Journal of Steroid Biochemistry and Molecular Biology. 185:80-89 |
| ISSN: | 0960-0760 |
| DOI: | 10.1016/j.jsbmb.2018.07.013 |
| Popis: | Many enzymes from the short-chain dehydrogenase/reductase superfamily (SDR) have already been well characterized, particularly those that participate in crucial biochemical reactions in the human body (e.g. 11β-hydroxysteroid dehydrogenase 1, 17β-hydroxysteroid dehydrogenase 1 or carbonyl reductase 1). Several other SDR enzymes are completely or almost completely uncharacterized, such as DHRS1 (also known as SDR19C1). Based on our in silico and experimental approaches, DHRS1 is described as a likely monotopic protein that interacts with the membrane of the endoplasmic reticulum. The highest expression level of DHRS1 protein was observed in human liver and adrenals. The recombinant form of DHRS1 was purified using the detergent n-dodecyl-β-D-maltoside, and DHRS1 was proven to be an NADPH-dependent reductase that is able to catalyse the in vitro reductive conversion of some steroids (estrone, androstene-3,17-dione and cortisone), as well as other endogenous substances and xenobiotics. The expression pattern and enzyme activities fit to a role in steroid and/or xenobiotic metabolism; however, more research is needed to fully clarify the exact biological function of DHRS1. |
| Databáze: | OpenAIRE |
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