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First discovered in rat liver over 60 years ago, the cytosolic glutathione S-transferases (GSTs) are a family of dimeric enzymes that have evolved to conjugate hydrophobic and electrophilic substrates to glutathione, resulting in their inactivation and significantly increased water solubility - thus facilitating their elimination from the body. Substrates for GSTs include a broad range of endogenous and xenobiotic substances, including byproducts of oxidative stress, carcinogens and therapeutic drugs.

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Dual approaches are efficient for improving the yield and functionality of APs, but cost scalability is a major factor limiting the adoption of these approaches