Human Glutathione Transferase T2-2 Discloses Some Evolutionary Strategies for Optimization of Substrate Binding to the Active Site of Glutathione Transferases
Open Access
- 1 February 2001
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (8) , 5427-5431
- https://doi.org/10.1074/jbc.m002819200
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine Residue of Human Mu Class Glutathione S-TransferasesPublished by Elsevier ,2000
- Fast Product Formation and Slow Product Release Are Important Features in a Hysteretic Reaction Mechanism of Glutathione Transferase T2-2Biochemistry, 1999
- Mutagenic analysis of conserved arginine residues in and around the novel sulfate binding pocket of the human Theta class glutathione transferase T2‐2Protein Science, 1999
- Proton Release upon Glutathione Binding to Glutathione Transferase P1-1: Kinetic Analysis of a Multistep Glutathione Binding ProcessBiochemistry, 1998
- Catalytic Mechanism and Role of Hydroxyl Residues in the Active Site of Theta Class Glutathione S-TransferasesPublished by Elsevier ,1997
- Structure, Catalytic Mechanism, and Evolution of the Glutathione TransferasesChemical Research in Toxicology, 1997
- X‐ray crystal structures of cytosolic glutathione S‐transferasesEuropean Journal of Biochemistry, 1994
- Structure and function of glutathione S-transferasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- Structure Determination and Refinement of Human Alpha Class Glutathione Transferase A1-1, and a Comparison with the Mu and Pi Class EnzymesJournal of Molecular Biology, 1993
- Effect of evolution on the kinetic properties of enzymesEuropean Journal of Biochemistry, 1989