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  • Ismail, Aram, et al. (author)
  • Marmoset glutathione transferases with ketosteroid isomerase activity
  • 2021
  • In: Biochemistry and Biophysics Reports. - : Elsevier BV. - 2405-5808. ; 27
  • Journal article (peer-reviewed)abstract
    • The common marmoset Callithrix jacchus encodes two glutathione transferase (GST) enzymes with ketosteroid double-bond isomerase activity. The most active enzyme is CjaGST A3-3 showing a specific activity with 5-androsten-3,17-dione (Delta(5)-AD) of 62.1 +/- 1.8 mu mol min(-1) mg(-1), and a k(cat) value of 261 +/- 49 s(-1). The second ketostemid isomerase CjaGST A1-1 has a 30-fold lower specific activity with Delta(5)-AD and a 37-fold lower k(cat) value. Thus, the marmoset CjaGST A3-3 would be the main contributor to the biosynthesis of the steroid hormones testosterone and progesterone, like the human ortholog HsaGST A3-3. Two residues differ in the H-site of the 91.4% sequence identical CjaGST A1-1 and CjaGST A3-3, and modeling of the structures suggests that the bulky phenyl ring of Phe111 in CjaGST A1-1 causes steric hindrance in the binding of the steroid substrate. Tributyltin acetate (IC50 =0.16 +/- 0.004 mu M) and ethacrynic acid (IC50 =3.3 +/- 0.2 mu M) were found to be potent inhibitors of CjaGST A3-3, as previously demonstrated with the human and equine orthologs.
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  • Result 1-1 of 1
Type of publication
journal article (1)
Type of content
peer-reviewed (1)
Author/Editor
Mannervik, Bengt (1)
Ismail, Aram (1)
Sawmi, Julia (1)
University
Stockholm University (1)
Language
English (1)
Research subject (UKÄ/SCB)
Natural sciences (1)
Year

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