EC Number   |
Reaction |
Reference |
|---|
    2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
active site involving residue Trp234, and substrate binding structure, isozyme GST T1-1 |
675362 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
active site structure and catalytic mechanism, overview |
721739 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
active site structure: Tyr111 indirectly stabilizes glutathione binding, Tyr119 modulates hydrophobic substrate binding, and Phe123 indirectly modulates catalysis. An aromatic zipper in the H-site contributing a network of aromatic pi-pi interactions. Several residues of the cluster directly interact with the hydrophobic substrate while others indirectly maintain conformational stability of the dimeric structure through the C-terminal domain II |
702150 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
catalytic mechanism of isozyme GSTH1-1 |
-, 723556 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
catalytic mechanism of kappa class GST, overview. Substrate binding induces a conformational change of the active site from an open conformation in the apo-form to a closed conformation in the S-hexylglutathione-bound complex, facilitating formations of the G site (GSH-binding site) and the H site (hydrophobic substrate-binding site). The conserved Ser16 at the G site functions as the catalytic residue in the deprotonation of the thiol group and the conserved Asp69, Ser200,Asp201 andArg202 form a network of interactions with gamma -glutamyl carboxylate to stabilize the thiolate anion. The H site is a large hydrophobic pocket with conformational flexibility to allow the binding of different hydrophobic substrates. The kinetic mechanism of hGSTk conforms to a rapid equilibrium random sequential Bi Bi model |
721532 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
catalytic mechanism, ovverview |
721709 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
kinetic mechanism |
637941, 637944 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
mechanism |
637905, 637940, 637952 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
mechanisms for formation of specific mono(glutathionyl) or bis(glutathionyl) conjugates |
672453 |
| 2.5.1.18 | RX + glutathione = HX + R-S-glutathione |
random steady state mechanism |
637923 |
