Structural contributions of Delta class glutathione transferase active-site residues to catalysis

Chemical Compounds

• Glutathione 74%
• S-Hexylglutathione 73%
• Mutation 70%
• 1-chloro-2,4-dinitrobenzene 61%
• Catalysis 53%
• Enzyme Kinetics 50%
• Xenobiotic Agent 48%
• Toxic Substance 45%
• Site-Directed Mutagenesis 43%
• Crystal Structure 41%
• Communication 37%
• Molecular Cluster 27%
• Protein 17%

Medicine & Life Sciences

• Catalysis 100%
• Glutathione Transferase 88%
• Catalytic Domain 75%
• Binding Sites 64%
• Enzymes 45%
• hexylglutathione 41%
• Kinetics 30%
• Dinitrochlorobenzene 28%
• Molecular Structure 25%
• Protein Stability 24%
• Biotransformation 24%
• Mutation 23%
• Xenobiotics 22%
• Site-Directed Mutagenesis 22%
• Poisons 15%