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Literature summary extracted from

  • Musci, G.; Bellenchi, G.C.; Calabrese, L.
    The multifunctional oxidase activity of ceruloplasmin as revealed by anion binding studies (1999), Eur. J. Biochem., 265, 589-597.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.16.3.1
-
 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.16.3.1 N3- anion behaves as an inhibitor of the oxidase activity versus Fe2+ Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.16.3.1 Cu2+
-
 Homo sapiens
1.16.3.1 Cu2+
-
 Gallus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.16.3.1 Fe2+ + H+ + O2 Homo sapiens
-
 Fe3+ + H2O
-
 ?
1.16.3.1 Fe2+ + H+ + O2 Gallus sp.
-
 Fe3+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.16.3.1 Gallus sp.
-
 chicken
-
1.16.3.1 Homo sapiens
-
 human
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.16.3.1
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.3.1 Fe2+ + H+ + O2
-
 Homo sapiens Fe3+ + H2O
-
 ?
1.16.3.1 Fe2+ + H+ + O2
-
 Gallus sp. Fe3+ + H2O
-
 ?
1.16.3.1 ferrous ammonium sulfate + O2
-
 Homo sapiens ?
-
 ?
1.16.3.1 p-phenylenediamine + Fe2+ + O2
-
 Homo sapiens ?
-
 ?
1.16.3.1 p-phenylenediamine + Fe2+ + O2
-
 Gallus sp. ?
-
 ?