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Literature summary for 1.16.3.4 extracted from

  • Kim, C.; Lorenz, W.; Hoopes, J.; Dean, J.
    Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene (2001), J. Bacteriol., 183, 4866-4875 .
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
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 Fe2+ pH 5, 30°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
copper contains six copper atoms per polypeptide chain and displays optical and electron paramagnetic resonance spectra consistent with the presence of type 1, type 2, and type 3 copper centers. The addition of copper leads to immediate and reversible changes in the optical and electron paramagnetic resonance spectra of the protein, as well as decreased thermal stability of the enzyme and stimulates both the phenoloxidase and ferroxidase activities Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P36649
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 Fe2+ + 4 H+ + O2 reaction of EC 1.16.3.1 Escherichia coli 4 Fe3+ + 2 H2O
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 ?
additional information enzyme additionally displays phenoloxidase activity, reaction of EC 1.10.3.2. Presence of Fe2+ reduces the apparent phenoloxidase activity, Cu(II) enhances this activity six- to sevenfold Escherichia coli ?
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