Glutathione S-transferase

spinqualitylabelsall models Glutathione S-tansferase complex with glutathione (PDB entry 1fhe) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione (GSH) to a variety of exogenous and endogenous hydrophobic electrophiles. For example, GST can detoxify peroxidised lipids. All eukaryotes possess a variety of GSTs with catalytic and non-catalytic activities. GST is divided into classes: α, δ, ε, κ, μ, ν, ω, π, ρ, σ (hematopoietic prostaglandin D synthase), τ, χ, ϑ, ζ and microsomal. epsilon glutathione S-transferase has a role in insecticide resistance. kappa glutathione S-transferase is found in mitochondria and peroxisomes. It may be involved in lipid metabolism. mu glutathione S-transferase detoxify carcinogens in tobacco smoke. nu glutathione S-transferase breaks the beta-aryl ether bond of lignin. pi glutathione S-transferase has a role in carcinogenic processes. rho glutathione S-transferase detoxifies water from the pollutant dichloroacetate. sigma glutathione S-transferase is a detoxifying agent providing drug resistance and acting as vaccine antigen. omega glutathione S-transferase catalyzes a range of thiol transferase reactions like biotransformation of haloketones to nontoxic acetophenones. zeta glutathione S-transferase catalyzes the reaction of glutathione with Endo- and xenobiotics. tau glutathione S-transferase and LanCL1 glutathione S-transferase are involved in oxidative stress response. phi glutathione S-transferase is plant-specific. microsomali glutathione S-transferase protects cells from cytostatic drugs and from oxidative stress. Relevance GST are targets for anti-diabetic drugs. Structural highlights The glutathione binding site is at the N-terminal of GST. 3D structures of glutathione S-transferase Glutathione S-transferase 3D structures

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