Microsomal glutathione S-transferase 1 (MGST1)

Microsomal glutathione S-transferase 1 (MGST1) is an integral membrane enzyme found abundantly in the endoplasmic reticulum, playing a critical role in cellular detoxification and oxidative stress protection[1][2][5][6]. It catalyzes the conjugation of glutathione to a variety of electrophilic substrates and reduces lipid hydroperoxides, thereby defending cells against both xenobiotics and oxidative damage[2][6]. MGST1 functions as a homotrimer, with its active site situated at the interface of subunits, and belongs to the MAPEG superfamily[1][4][5]. It is overexpressed in certain cancers, where it can mediate resistance to cytotoxic drugs, and its regulation is responsive to oxidative stress[3][6]. MGST1’s structural and catalytic properties make it a prototypical membrane-associated phase II detoxification enzyme, distinct from soluble cytosolic glutathione S-transferases[7].

Other names

MGST1Microsomal GST-IMAPEG glutathione S-transferase 1Membrane-associated protein in eicosanoid and glutathione metabolism 1

Catalyzes conjugation of **glutathione (GSH)** to a wide range of **electrophilic substrates**, including xenobiotics and products of oxidative stress Reduces **lipid hydroperoxides**, acting as a membrane-bound glutathione peroxidase