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Porcine glutathione...
Porcine glutathione transferase Alpha 2-2 is a human GST A3-3 analogue that catalyses steroid double-bond isomerization
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- Fedulova, Natalia, 1980- (författare)
- Uppsala universitet,Institutionen för biokemi och organisk kemi
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- Raffalli-Mathieu, Francoise (författare)
- Uppsala universitet,Institutionen för biokemi och organisk kemi
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- Mannervik, Bengt (författare)
- Uppsala universitet,Institutionen för biokemi och organisk kemi
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(creator_code:org_t)
- 2010
- 2010
- Engelska.
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Ingår i: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 431:1, s. 159-167
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- A primary role of GSTs (glutathione transferases) is detoxication of electrophilic compounds. In addition to this protective function, hGST (human GST) A3-3, a member of the Alpha class of soluble GSTs, has prominent steroid double-bond isomerase activity. The isomerase reaction is an obligatory step in the biosynthesis of steroid hormones, indicating a special role of hGST A3-3 in steroidogenic tissues. An analogous GST with high steroid isomerase activity has so far not been found in any other biological species. In the present study, we characterized a Sus scrofa (pig) enzyme, pGST A2-2, displaying high steroid isomerase activity. High levels of pGST A2-2 expression were found in ovary, testis and liver. In its functional properties, other than steroid isomerization, pGST A2-2 was most similar to hGST A3-3. The properties of the novel porcine enzyme lend support to the notion that particular GSTs play an important role in steroidogenesis.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Delta(5)-androstene-3
- 17-dione
- androstenedione
- double-bond isomerization
- glutathione transferase Alpha 2-2 (GST A2-2)
- steroidogenesis
- tributyltin
- Biochemistry
- Biokemi
- Biokemi
- Biochemistry
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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