Entropy-driven binding of picomolar transition state analogue inhibitors to Human 5′-methylthioadenosine phosphorylase

Medicine & Life Sciences

• 5'-methylthioadenosine phosphorylase 100%
• Entropy 67%
• 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A 47%
• Catalytic Domain 17%
• Thermodynamics 15%
• Purine-Nucleoside Phosphorylase 9%
• Water 8%
• Catalysis 7%
• Polyamines 7%
• Enzyme Inhibitors 7%
• Hydrophobic and Hydrophilic Interactions 6%
• Methionine 6%
• Hot Temperature 4%
• Proteins 4%
• Enzymes 3%
• Pharmaceutical Preparations 2%

Chemical Compounds

• Entropy 23%
• Enthalpy 22%
• Purine Nucleoside 18%
• Polyamine 15%
• Heat Capacity 14%
• Trimer 13%
• Protein 11%
• Transition State 11%
• Titration 10%
• Condensation 10%
• Catalysis 9%
• Thermodynamics 8%
• Drug 7%
• Crystal Structure 7%