Microsomal glutathione S-transferase 2 (MGST2)

Microsomal glutathione S-transferase 2 (MGST2) is a 17 kDa trimeric integral membrane enzyme of the MAPEG family involved in cellular detoxification, drug metabolism, and the regulation of inflammatory mediators[1][2][4][5]. MGST2 catalyzes glutathione-dependent reduction of lipid hydroperoxides and conjugation of electrophilic compounds (such as 1-chloro-2,4-dinitrobenzene or 4-hydroxy-2-nonenal) with glutathione, aiding in the metabolism and detoxification of xenobiotics and lipid peroxidation products[1][2][4]. Critically, in tissues where leukotriene C4 synthase (LTC4S) is absent, MGST2 serves as the main enzyme for the biosynthesis of the pro-inflammatory mediator leukotriene C4 (LTC4) from leukotriene A4 and glutathione[1][5]. MGST2 expression and activity are implicated in conditions associated with inflammation, oxidative stress, and DNA damage responses to ER stress or anticancer agents[2][4][5]. There are no current clinical inhibitors or therapeutics specifically targeting MGST2, though its central enzymatic roles make it of interest in pharmacology and toxicology.

Other names

GST2MGST-IIMicrosomal GST-2Microsomal GST-IIGlutathione peroxidase MGST2Leukotriene C4 synthase MGST2

Drugs or molecules that interact with MGST2 typically act as: Substrate analogs (e.g., CDNB, LTA4) that serve as electrophilic targets for conjugation with glutathione; Inhibitors that may block substrate binding, glutathione activation, or product formation. Not a current direct therapeutic target for marketed drugs, but inhibition could affect leukotriene C4 and inflammatory mediator formation.