Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | a multicopper oxidase | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 Fe(II) + 4 H+ + O2 | Homo sapiens | - |
4 Fe(III) + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 Fe(II) + 4 H+ + O2 | - |
Homo sapiens | 4 Fe(III) + 2 H2O | - |
? | |
additional information | development of the classic chromophoric complex FeIIHx(Tar)2 (H2Tar), 4-(2-thiazolylazo)-resorcinol (x = 0-2) as a robust substrate for evaluation of the ferroxidase function of ceruloplasmin and related enzymes. The catalysis can be followed conveniently in real-time by monitoring the solution absorbance at 720 nm, a fingerprint of FeIIHx(Tar)2. The complex is oxidized to its ferric form FeIIIHx(Tar)2. Fe(II) is transferred formally from FeIIHx(Tar)2 to the substrate docking/oxidation (SDO) site(s) in ceruloplasmin, followed by oxidation to product Fe(III) that is trapped again by the ligand. Each Tar ligand in the above bis-complex coordinates the metal center in a meridional tridentate mode involving a pH-sensitive -OH group (pKa >12), and this imposes rapid Fe(II) and Fe(III) transfer kinetics to facilitate the catalytic process. Method evaluation and proposed mechanism, detailed overview | Homo sapiens | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
ceruloplasmin | - |
Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | ceruloplasmin is one of the most complex multicopper oxidase enzymes and plays an essential role in the metabolism of iron in mammals. Ferrous ion supplied by the ferroportin exporter is converted by ceruloplasmin to ferric ion that is accepted by plasma metallo-chaperone transferrin. The multicopper oxidase enzymes mediate transfer of the iron from the cell export pump ferroportin to the plasma metallo-chaperone transferrin. Specifically, they are responsible for conversion of Fe(II) to Fe(III), the form in which it is transported in the blood by transferrin | Homo sapiens |