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Zemanová, L.* ; Navrátilová, H.* ; Andrýs, R.* ; Šperková, K.* ; Andrejs, J.* ; Kozáková, K.* ; Meier, M. ; Möller, G. ; Novotná, E.* ; Šafr, M.* ; Adamski, J. ; Wsól, V.*

Initial characterization of human DHRS1 (SDR19C1), a member of the short chain dehydrogenase/reductase superfamily.

J. Steroid Biochem. Mol. Biol. 185, 80-89 (2019)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Dhrs1 ; Sdr19c1 ; Sdr Superfamily ; Steroid Hormones ; Xenobiotics; Subcellular-localization; Membrane-proteins; Lipid Droplets; Sdr; Reconstitution; Prediction; Identification; Purification; Classification; Cytoplasm
ISSN (print) / ISBN 0960-0760
e-ISSN 0960-0760
Journal Journal of Steroid Biochemistry and Molecular Biology, The
Quellenangaben Volume: 185, Issue: , Pages: 80-89 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place The Boulevard, Langford Lane, Kidlington, Oxford Ox5 1gb, England
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Experimental Genetics (IEG)