Initial characterization of human DHRS1 (SDR19C1), a member of the short-chain dehydrogenase/reductase superfamily
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
30031147
DOI
10.1016/j.jsbmb.2018.07.013
PII: S0960-0760(18)30186-9
Knihovny.cz E-zdroje
- Klíčová slova
- DHRS1, SDR superfamily, SDR19C1, Steroid hormones, Xenobiotics,
- MeSH
- dehydrogenasy/reduktasy s krátkým řetězcem metabolismus MeSH
- endoplazmatické retikulum metabolismus MeSH
- estron metabolismus MeSH
- HeLa buňky MeSH
- játra metabolismus MeSH
- kortison metabolismus MeSH
- lidé MeSH
- nadledviny metabolismus MeSH
- nádorové buněčné linie MeSH
- oxidoreduktasy genetika metabolismus MeSH
- rekombinantní proteiny biosyntéza genetika MeSH
- sekvence aminokyselin MeSH
- Sf9 buňky MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- dehydrogenasy/reduktasy s krátkým řetězcem MeSH
- DHRS1 protein, human MeSH Prohlížeč
- estron MeSH
- kortison MeSH
- oxidoreduktasy MeSH
- rekombinantní proteiny 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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