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Glutathione S-transferase enzymes can conjugate GSH to selected electrophiles, reactive metabolic products and xenobiotic compounds

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A structural explanation for these findings was provided from our previous cryo-EM structures of CT(Pro32) and rAmy(Tyr37)-bound AMYRs structures where the bulky phenolic side chain of Y37 rAmy forms perpendicular π stacking interactions with W79 ECD 15 , and additional interactions with the respective RAMP protomer that are likely important for selectivity of rAmy for AMYRs over CTR