Article
Isomerization of Δ5-androstene-3,17-dione into Δ4-androstene-3,17-dione catalyzed by human glutathione transferase A3-3: a computational study identifies a dual role for glutathione.
The journal of physical chemistry. A - 7 Aug 2014
Dourado Daniel F A R, Fernandes Pedro Alexandrino, Mannervik Bengt, Ramos Maria João
Abstract excerpt
Glutathione transferases (GSTs) are important enzymes in the metabolism of electrophilic xenobiotic and endobiotic toxic compounds. In addition, human GST A3-3 also catalyzes the double bond isomerization of Δ5-androstene-3,17-dione (Δ(5)-AD) and Δ(5)-pregnene-3,20-dione (Δ(5)-PD), which are the immediate precursors of testosterone and progesterone. In fact, GST A3-3 is the most efficient human enzyme known to...
Topics
- Amino Acid Sequence
- Androstenedione
- Biocatalysis
- Computer Simulation
- Crystallography, X-Ray
- Glutathione
- Glutathione Transferase
- Humans
- Isomerism
- Kinetics