Thermodynamic analysis of transition-state features in picomolar inhibitors of human 5′-methylthioadenosine phosphorylase

Medicine & Life Sciences

• 5'-methylthioadenosine phosphorylase 100%
• 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A 80%
• Thermodynamics 69%
• Phosphates 35%
• 5'-methylthioadenosine 28%
• Nitrogen 15%
• Purine-Nucleoside Phosphorylase 12%
• S-Adenosylmethionine 10%
• Entropy 9%
• Protein Stability 9%
• Catalytic Domain 7%
• Biochemistry 7%
• Ions 6%
• Hot Temperature 6%
• Enzymes 4%
• Proteins 2%

Chemical Compounds

• Transition State 46%
• Phosphate 20%
• Purine Nucleoside 8%
• Nitrogen 7%
• Biochemistry 5%
• Ion Pair 5%
• Binding Energy 5%
• Entropy 5%
• Enthalpy 4%
• Pharmacological Metabolism 4%
• Gibbs Free Energy 4%
• Thermal Stability 4%
• Thermodynamics 3%
• Protein 2%