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Inhibition characteristics of equine steroid isomerase EcaGST A3-3
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- Lindström, Helena (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Mazari, Aslam M. A. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Musdal, Yaman (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- English.
- Other publication (other academic/artistic)
Abstract
Subject headings
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- Equine glutathione transferase A3-3 (EcaGST A3-3) belongs to the superfamily of detoxifying enzymes found in all organisms. However it is also the most efficient steroid double-bond isomerase known in mammals. In contrast to the rodents, Equus ferus caballus shares the steroidogenic pathway with Homo sapiens, which makes it a more suitable model for human steroidogenesis than the murine one. Inhibition of EcaGST A3-3 might help treat reproductive and neurodegenerative disorders. We screened an FDA-approved library of 1040 compounds for the ability as novel inhibitors of EcaGST A3-3. Our results revealed anthralin, sennoside A, tannic acid and ethacrynic acid as the most potent, submicromolar-range inhibitors of EcaGST A3-3 with the natural substrate Δ5-androstene-3,17-dione.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Steroidogenesis
- Inhibition
- Catalytic efficiency
- Glutathione transferase A3-3
- Androstenedione
- Pregnenedione
- Glutahione transferase M2-2
- neurokemi med molekylär neurobiologi
- Neurochemistry with Molecular Neurobiology
Publication and Content Type
- vet (subject category)
- ovr (subject category)
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- Mannervik, Bengt
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