Glutathione S-transferase Mu 2 (GSTM2)

Glutathione S-transferase Mu 2 (GSTM2) is an enzyme of the mu class within the glutathione S-transferase superfamily, primarily found in the cytosol. It catalyzes the conjugation of reduced glutathione to a broad range of endogenous and exogenous hydrophobic electrophiles, thereby facilitating detoxification, scavenging reactive species, and protecting cells from oxidative stress. GSTM2 also plays specialized roles in lipid metabolism regulation and inhibits cell death signaling by binding to ASK1. The gene is highly polymorphic, which contributes to individual variability in susceptibility to carcinogens, drug toxicity, and metabolic diseases such as hepatic steatosis[1][2][4][6].

Other names

GSTM2Mu class GSTGlutathione S-transferase M2

Conjugation of reduced glutathione to hydrophobic electrophiles, increasing solubility and facilitating excretion; Protection from oxidative stress by scavenging reactive oxygen species; Inhibition of stress kinases (ASK1, JNK), impacting cell survival signaling