Initial characterization of human DHRS1 (SDR19C1), a member of the short-chain dehydrogenase/reductase superfamily
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
30031147
DOI
10.1016/j.jsbmb.2018.07.013
PII: S0960-0760(18)30186-9
Knihovny.cz E-resources
- Keywords
- DHRS1, SDR superfamily, SDR19C1, Steroid hormones, Xenobiotics,
- MeSH
- Short Chain Dehydrogenase-Reductases metabolism MeSH
- Endoplasmic Reticulum metabolism MeSH
- Estrone metabolism MeSH
- HeLa Cells MeSH
- Liver metabolism MeSH
- Cortisone metabolism MeSH
- Humans MeSH
- Adrenal Glands metabolism MeSH
- Cell Line, Tumor MeSH
- Oxidoreductases genetics metabolism MeSH
- Recombinant Proteins biosynthesis genetics MeSH
- Amino Acid Sequence MeSH
- Sf9 Cells MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Short Chain Dehydrogenase-Reductases MeSH
- DHRS1 protein, human MeSH Browser
- Estrone MeSH
- Cortisone MeSH
- Oxidoreductases MeSH
- Recombinant Proteins MeSH
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.
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