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Literature summary for 3.4.11.10 extracted from
- The slow, tight binding of bestatin and amastatin to aminopeptidases (1985), J. Biol. Chem., 260, 13154-13162.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| amastatin | reversible, slow, tight binding, transition state analog complex, Ki: 0.58 nM, stoichiometry of inhibition 1:1 | Vibrio proteolyticus |  |
| bestatin | reversible, slow, tight binding, transition state analog complex, Ki: 18 nM, stoichiometry of inhibition 1:1 | Vibrio proteolyticus | |
| epibestatin | Ki: 0.07 mM | Vibrio proteolyticus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Peptides + H2O | Vibrio proteolyticus | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vibrio proteolyticus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Peptides + H2O | - |
Vibrio proteolyticus | ? | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Vibrio proteolyticus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Vibrio proteolyticus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.000058 | - |
amastatin | reversible, slow, tight binding, transition state analog complex, stoichiometry of inhibition 1:1 | Vibrio proteolyticus | |
| 0.07 | - |
epibestatin | - |
Vibrio proteolyticus | |
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