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Literature summary for 3.4.11.18 extracted from
- Protonation states of methionine aminopeptidase and their relevance for inhibitor binding and catalytic activity (2003), J. Biol. Chem., 278, 47862-47867.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| fumagillin | irreversible | Escherichia coli |  |
| additional information | one of the protomeric states of the enzyme is relevant for inhibitor binding, whereas the other is relevant for substrate hydrolysis | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AE18 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Met-Gly-Met-Met + H2O | - |
Escherichia coli | Gly-Met-Met + Met | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
reaction with Met-Gly-Met-Met | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 8 | pH 6.5: about 30% of maximal activity, pH 8.0: about 25% of maximal activity | Escherichia coli |
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Release 2023.1 (January 2023)
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