A comparison of the structures and kinetic properties of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) and its mutant enzymes (Leu308Val and Leu308Ala) indicates that Leu308 is a selectivity determinant for substrate binding. While the Leu308Val mutation improved the catalytic efficiency (k(cat)/K(m)) of
Journal of medicinal chemistry, 49(5), 1818-1827 (2006-03-03)
A set of 28 enantiomers comprising rigid and flexible secondary alcohols was synthesized by the asymmetric Corey-Bakshi-Shibata reduction. The enantiomerically pure alcohols were subjected to enzymatic glucuronidation assays employing the human UDP-glucuronosyltransferases (UGTs) 2B7 and 2B17. Both UGTs displayed high
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