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Updated: Aug 13, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Human glutathione transferase A3-3 active as steroid double-bond isomerase
Françoise Raffalli-Mathieu1, Bengt Mannervik
1Department of Biochemistry, Uppsala University Biomedical Center, Sweden.
Abstract:
Glutathione transferases (GSTs) constitute a superfamily of detoxifying enzymes with a major role in protecting cellular macromolecules from reactive electrophilic compounds. A growing body of evidence suggests, however, that at least certain glutathione transferases are involved in other essential cellular processes, such as cellular signaling and anabolic pathways. One of them is the human GST A3-3, which is selectively expressed in steroidogenic organs and which efficiently catalyzes the obligatory isomerization of the Delta(5)-ketosteroid precursors in the biosynthesis of progesterone and testosterone. In this chapter, we summarize the current knowledge on human GST A3-3 and describe methods for heterologous expression and functional characterization of the enzyme.
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