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Potent inhibitors of equine steroid isomerase EcaGST A3-3
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-0236-1796
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 42019 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 14, no 3, article id e0214160Article in journal (Refereed) Published
Abstract [en]

Equine glutathione transferase A3-3 (EcaGST A3-3) belongs to the superfamily of detoxication enzymes found in all higher organisms. However, it is also the most efficient steroid double-bond isomerase known in mammals. Equus ferus caballus shares the steroidogenic pathway with Homo sapiens, which makes the horse a suitable animal model for investigations of human steroidogenesis. Inhibition of the enzyme has potential for treatment of steroid-hormone-dependent disorders. Screening of a library of FDA-approved drugs identified 16 out of 1040 compounds, which at 10 mu M concentration afforded at least 50% inhibition of EcaGST A3-3. The most potent inhibitors, anthralin, sennoside A, tannic acid, and ethacrynic acid, were characterized by IC50 values in the submicromolar range when assayed with the natural substrate Delta(5)-androstene-3,17-dione.

Place, publisher, year, edition, pages
2019. Vol. 14, no 3, article id e0214160
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Biological Sciences
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URN: urn:nbn:se:su:diva-168366DOI: 10.1371/journal.pone.0214160ISI: 000461889700075PubMedID: 30897163OAI: oai:DiVA.org:su-168366DiVA, id: diva2:1314398
Available from: 2019-05-08 Created: 2019-05-08 Last updated: 2019-05-08Bibliographically approved

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