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Literature summary for 2.4.2.1 extracted from
- Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase (2009), Biochemistry, 48, 5226-5238.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | thermodynamics for binding the immucillins to the first subunit of human purine nucleoside phosphorylase. Titrations of purine nucleoside phosphorylase using isothermal calorimetry indicate that binding of a structurally rigid first-generation immucillin-H is driven by large negative enthalpy values with a substantial entropic penalty. The tightest-binding inhibitors have increased conformational flexibility. Despite their conformational freedom in solution, flexible inhibitors bind with high affinity because of reduced entropic penalties. Entropic penalties are proposed to arise from conformational freezing of the purine nucleoside phosphorylase-inhibitor complex with the entropy term dominated by protein dynamics. The conformationally flexible immucillins reduce the system entropic penalty. Disrupting the ribosyl 5'-hydroxyl interaction of transition state analogues with purine nucleoside phosphorylase causes favorable entropy of binding. Tight binding of the immucillins is characterized by large enthalpic contributions, emphasizing their similarity to the transition state | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P00491 | - |
- |
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Release 2023.1 (January 2023)
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