MGST2 (microsomal glutathione S-transferase 2) is a 17 kDa trimeric integral membrane protein that catalyzes multiple glutathione-dependent reactions 1. Its primary function is LTC4 biosynthesis, conjugating leukotriene A4 with reduced glutathione to form leukotriene C4 1, though with lower catalytic efficiency (1.8 × 10⁴ M⁻¹ s⁻¹) compared to dedicated LTC4 synthase 1. MGST2 also exhibits glutathione peroxidase activity toward lipid hydroperoxides and glutathione transferase activity toward xenobiotic electrophiles like 1-chloro-2,4-dinitrobenzene 1. Mechanistically, MGST2 employs synchronized conformational changes regulating catalysis, with the trimeric structure restricting active-site availability 2. Clinically, MGST2-mediated LTC4 production is implicated in drug-induced nephrotoxicity and ER stress-induced oxidative DNA damage, with LTC4 triggering NADPH oxidase 4-mediated cell death in kidney cells 3. Recent studies demonstrate MGST2 involvement in inflammatory resolution through production of specialized proresolving mediators 4. Additionally, MGST2 upregulation correlates with hepatitis B virus-induced carcinogenesis 5, suggesting disease relevance beyond inflammatory contexts.