Initial characterization of human DHRS1 (SDR19C1), a member of the short chain dehydrogenase/reductase superfamily
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F19%3A50014961" target="_blank" >RIV/62690094:18470/19:50014961 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11150/19:10400934 RIV/00216208:11160/19:10400934 RIV/00179906:_____/19:10400934
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0960076018301869" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0960076018301869</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jsbmb.2018.07.013" target="_blank" >10.1016/j.jsbmb.2018.07.013</a>
Alternative languages
Result language
angličtina
Original language name
Initial characterization of human DHRS1 (SDR19C1), a member of the short chain dehydrogenase/reductase superfamily
Original language description
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. 11 beta-hydroxysteroid dehydrogenase 1, 17 beta-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 ndodecy1-beta-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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of steroid biochemistry and molecular biology
ISSN
0960-0760
e-ISSN
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Volume of the periodical
185
Issue of the periodical within the volume
January
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
80-89
UT code for WoS article
000453489900009
EID of the result in the Scopus database
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