Glutathione S-transferase theta-2B (GSTT2B)

Glutathione S-transferase theta-2B (GSTT2B) is an enzyme encoded by the GSTT2B gene, part of the glutathione S-transferase (GST) superfamily, which includes alpha, mu, pi, theta, and zeta classes[1][4][3]. GSTs catalyze the conjugation of reduced glutathione to exogenous and endogenous electrophilic and hydrophobic compounds, facilitating their detoxification and excretion from the cell[1][2]. The theta class, which includes GSTT1, GSTT2, and GSTT2B, is important in cellular defense against oxidative stress and xenobiotic insult. GSTT2B has some genetic ambiguity: it is a protein-coding gene but has been described as a pseudogene in certain populations, potentially impacting its function[1]. Disease associations include roles in various inherited disorders and a possible influence in susceptibility to carcinogenesis and inflammatory diseases due to its detoxification role and genetic polymorphism[1][2][3]. GSTT2B is cytosolic and, like other GSTs, is implicated in phase II biotransformation pathways. The molecular mechanism involves nucleophilic addition or substitution of glutathione to electrophilic centers, driven by conserved residues in the active site[2][3]. Drugs that induce or inhibit GSTs or interact with glutathione metabolism could theoretically influence GSTT2B function, although no specific drug interactions are currently attributed directly to this protein in literature[1][4].

Other names

Glutathione S-transferase theta-2GST class-theta-2GSTT2GSTT2Pglutathione S-transferase theta 2

GSTT2B catalyzes drug detoxification via glutathione conjugation and subsequent excretion. It likely contributes to resistance against chemotherapeutic agents and environmental toxins. The molecular mechanism involves nucleophilic addition or substitution of glutathione to electrophilic centers, driven by conserved residues in the active site.