Glutathione S-transferase theta-2 (GSTT2)

Glutathione S-transferase theta-2 (GSTT2) is a member of the theta class of cytosolic glutathione S-transferases, a superfamily of detoxification enzymes involved in the conjugation of reduced glutathione to a wide variety of endogenous and exogenous electrophiles, facilitating their solubilization and elimination from the cell. GSTT2 differs structurally from other GSTs by having a unique C-terminal extension that deeply buries the substrate-binding pocket and contributes to a novel sulfate-binding site, thereby conferring distinctive substrate selectivity, including specific sulfatase activity. Highly expressed in cytosolic compartments, GSTT2 is thought to play a role in modulating susceptibility to carcinogenesis and drug resistance due to its involvement in xenobiotic metabolism. The GSTT2 gene is located on chromosome 22q11.23 and is structurally similar to GSTT1, with the two encoding enzymes sharing about 55% amino acid sequence identity. In humans, GSTT2 is one of 18 GSTs and, like other GSTs, is implicated in cellular defense, although its precise endogenous substrates and physiological roles remain incompletely characterized.

Other names

GSTT2Glutathione S-transferase theta 2GST class-theta-2glutathione S-transferase theta-2

Enzyme inhibition (e.g., by inhibitors), enzyme activation or substrate (e.g., glutathione conjugation with cytotoxic compounds)