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The superfamily of glutathione transferases (GSTs) comprises several distinct and multifunctional proteins widely distributed in Nature among eukaryotes and prokaryotes. GSTs are divided according to their cellular localization, with the cytosolic GSTs largely distributed in eukaryotes and further subgrouped into seven distinct classes of enzymes (Mannervik et al., 2005; Board and Menon, 2013). Besides the early recognized involvement of GSTs in the metabolism of drugs and xenobiotics, a growing number of data has revealed other biological functions of GSTs. These include isomerase reactions, protein glutathionylation, and the regulation of signaling pathways (Board and Menon, 2013). Non-enzymatic functions, including the regulation of the MAPK pathway (Adler et al., 1999; Pljesa-Ercegovac et al., 2018) and ryanodine receptors (Dulhunty et al., 2011), have also been proposed for some GSTs. During recent years, the interest in GSTs has increased due to their involvement in varied fields of biology and medicine. Moreover, the development of specific GST inhibitors has become an active topic of study. The reviews and research articles of the present Research Topic represent an attempt to focus on the novel, not yet fully explored mechanisms and functions of GSTs. Mannervik and colleagues review the ketosteroid isomerase activity of GSTs in the first manuscript of this research topic. The authors summarize and discuss studies about the contribution of alpha-class GSTs (GSTA) to steroid hormone biosynthesis in mammalian tissues. Human GSTA3-3 and GSTA1-1 isoforms support the activity of the 3β-hydroxysteroid dehydrogenase …