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Literature summary for 3.4.23.22 extracted from
- Binding of phosphinate and phosphonate inhibitors to aspartic proteases: a first-principles study (2006), J. Phys. Chem. B, 110, 1437-1442.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure of enzyme bound to inhibitor Pd130328, inhibitor binding structure and analysis | Cryphonectria parasitica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | molecular mechanism of enzyme inhibition by phosphinate and phosphonate inhibitors, molecular dynamic simulations for investigation of the hydrogen bonding pattern, structure, overview | Cryphonectria parasitica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cryphonectria parasitica | - |
i.e. Cryphonectria parasitica | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk | the enzyme contains a catalytic Asp dyad | Cryphonectria parasitica |
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Release 2023.1 (January 2023)
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