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[1].
- epsilon glutathione S-transferase has a role in insecticide resistance[2].
- kappa glutathione S-transferase is found in mitochondria and peroxisomes. It may be involved in lipid metabolism[3].
- mu glutathione S-transferase detoxify carcinogens in tobacco smoke[4].
- nu glutathione S-transferase breaks the beta-aryl ether bond of lignin[5].
- pi glutathione S-transferase has a orle in carcinogenic processes[6].
- rho glutathione S-transferase detoxifies water from the pollutant dichloroacetate[7].
- sigma glutathione S-transferase is a detoxifying agent providing drug resistance and acting as vaccine antigen[8].
- omega glutathione S-transferase catalyzes a range of thiol transferase reactions like biotransformation of haloketones to nontoxic acetophenones[9].
- zeta glutathione S-transferase catalyzes the reaction of glutathione with Endo- and xenobiotics[10].
Relevance
GST are targets for anti-diabetic drugs.
Structural highlights
The [11].
3D structures of glutathione S-transferase
Glutathione S-transferase 3D structures
