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Literature summary for 3.4.11.18 extracted from

  • D'Souza, V.M.; Bennett, B.; Copik, A.J.; Holz, R.C.
    Divalent Metal Binding Properties of the Methionyl Aminopeptidase from Escherichia coli (2000), Biochemistry, 39, 3817-3826.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ maximal activity is observed after addition of only 1 equivalent of divalent metal ion, the metal binding constant for the first binding event is 0.0003 mM for Co(II)-substituted enzyme. The metal ion resides in a pentacoordinate geometry Escherichia coli
Fe2+ maximal activity is observed after addition of only 1 equivalent of divalent metal ion, the metal binding constant for the first binding event is 0.0002 mM for Fe(II)-substituted enzyme. The metal ion resides in a pentacoordinate geometry Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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