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Literature summary for 3.4.11.18 extracted from
- Structural basis of catalysis by monometalated methionine aminopeptidase (2006), Proc. Natl. Acad. Sci. USA, 103, 9470-9475.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| mono- and dimetalated enzyme in complex with transition state analog norleucine phosphonate | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activation requires only one equivalent of Co2+ or Mn2+ | Escherichia coli |  |
| Mn2+ | activation requires only one equivalent of Co2+ or Mn2+ | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AE18 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| release of N-terminal amino acids, preferentially methionine, from peptides and arylamides | reaction mechanism of monometalated enzyme. Charge-charge interactions involving D97 and D108 position and bind substrate. E204 acts as general base | Escherichia coli |
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Release 2023.1 (January 2023)
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