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• W4240020903 abstract "Abstract Ceruloplasmin is a multi‐copper oxidase that contains most of the copper present in the plasma. It is an acute‐phase reactant that exhibits a two‐ to three‐fold increase over the normal concentration of 300 mg ml −1 in adult plasma. However, the precise physiological role(s) of ceruloplasmin has been the subject of intensive debate and it is likely that the enzyme has a multi‐functional role, including iron oxidase activity and oxidation of biogenic amines. The three‐dimensional X‐ray structure of the human enzyme shows that the molecule is composed of six cupredoxin‐type domains arranged in a triangular array. There are six integral copper atoms per molecule (mononuclear sites in domains 2, 4, and 6 and a trinuclear site between domains 1 and 6) and two labile sites with roughly 50% occupancy. Further structural studies on the binding of metal cations by the enzyme have indicated a putative mechanism for ferroxidase activity. Other studies have located the binding sites for an inhibitor (azide) and various substrates [aromatic diamines, biogenic amines, and D ‐lysergic acid diethylamide (LSD)]. The binding site of the azide moiety is topologically equivalent to one of the sites reported for ascorbate oxidase. However, there are two distinct binding sites for amine substrates; aromatic diamines bind at the base of domain 4 remote from the mononuclear copper site, whereas the biogenic amine series typified by serotonin, epinephrine, and dopa bind in close vicinity to that site utilized by cations in domain 6 and close to the mononuclear copper." @default.
• W4240020903 created "2022-05-12" @default.
• W4240020903 creator A5087566573 @default.
• W4240020903 date "2004-03-05" @default.
• W4240020903 modified "2023-09-29" @default.
• W4240020903 title "Ceruloplasmin" @default.
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• W4240020903 doi "https://doi.org/10.1002/0470028637.met200" @default.
• W4240020903 hasPublicationYear "2004" @default.
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