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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • 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

  • 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