User:Johanna Spaniol/Sandbox 1
From Proteopedia
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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 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 N-terminal region (80residues), a C-terminal extension comprising two helices connected by a long loop and a specific <scene name='User:Johanna_Spaniol/Sandbox_1/Sulfate_binding_site/1'>sulfatase activity</scene>. The extension completely buries the substrate-binding pocket and occludes most of the glutathione-binding site. | + | The protein has a <scene name='User:Johanna_Spaniol/Sandbox_1/N-terminal_domain/1'>N-terminal region</scene> (80residues), a C-terminal extension comprising two helices connected by a long loop and a specific <scene name='User:Johanna_Spaniol/Sandbox_1/Sulfate_binding_site/1'>sulfatase activity</scene>. 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. | 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. | ||
Revision as of 19:19, 6 January 2013
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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 N-term binding interface and a C-term binding interface. 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.
