User:Johanna Spaniol/Sandbox 1
From Proteopedia
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Glutathione S-Transferase form a wide family of enzymes divided in mammals into 5 classes (alpha, mu, pi, sigma and theta). These enzymes are involved in the cellular detoxification : they reduce the reactivity of toxic compounds by catalysing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents (green link). Gluthathione theta class S-Transferase is an enzyme member of the GTS family, located in hepatic cells of procaryotes and eucaryotes in the cytosol and in mitochondrias. This enzyme is a dimeric protein of 45-55kDa. The two subunits are encountered: the of the first subunit is in contact with the N-terminal domain of the 2nd subunit. So each subunit has an and a . The two subunits form the dimeric protein and there are some specific residues forming the dimer interface (N-terminal and C-terminal dimer interface).
The protein has a (80residues), a C-terminal extension comprising two helices connected by a long loop and a specific . The extension completely buries the substrate-binding pocket and occludes most of the glutathione-binding site.
A narrow tunnel leading from the active site to the surface may provide a pathway for the entry of substrates and the release of products.
