Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ceruloplasmin, the blue copper-protein of the blood plasma, is believed by some workers to be involved in the metabolic management of 5-hydroxytryptamine (serotonin) during pregnancy. 5-Hydroxytryptamine is abortifacient in experimental animals. By some authors, a role has been suggested for it in human abortion. The plasma concentrations of 5-hydroxytryptamine, copper and ceruloplasmin were measured in non-pregnant women, in normal early pregnancy and in cases of spontaneous abortion. Compared with normal early pregnancy, cases of inevitable abortion show lower values for both plasma copper and ceruloplasmin and higher values for plasma 5-hydroxytryptamine. The possible implications of these findings are discussed in view of the alterations in ceruloplasmin values in pregnancy and in the light of what is known of the pharmacology and metabolism of 5-hydroxytryptamine. It it believed that these alterations in plasma copper, ceruloplasmin and 5-hydroxytryptamine in cases of inevitable abortion are the effect, rather than the cause, of abortion.
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PMID:5-Hydroxytryptamine (serotonin), copper and ceruloplasmin plasma concentrations in spontaneous abortion. 26 87

The oxidation chemistry and biochemistry of the serotonergic neurotoxin 5,7-dihydroxytryptamine (1) has been studied under anaerobic and aerobic conditions in aqueous solution at physiological pH. Under anaerobic conditions, one-electron oxidants (ferricytochrome c, peroxidase/H2O2, ceruloplasmin, Cu2+) generate a radical intermediate. Dimerization of the C(6)-centered resonance form of this radical followed by secondary oxidations yields 3-(2-aminoethyl)-6-[3-(2-aminoethyl)-1,7-dihydro- 5-hydroxy-7-oxo-6H-indol-6-ylidene]-1-H-indole-5,7(4H,6H)-dione. Under aerobic conditions, molecular O2 attacks the C(4)-centered 1 radical to yield a hydroperoxy radical which decomposes to 5-hydroxytryptamine-4,7-dione (2). Autoxidation of 1 proceeds by primary attack by molecular O2 on a C(4)-centered carbanion to form a superoxide-radical complex. This rearranges to a C(4)-centered hydroperoxide which decomposes to 2. A C(6)-centered carbanion of 1 combines with 2 to give, ultimately, 6,6'-bi-5-hydroxytryptamine-4,7-dione (3). Trace concentrations of transition metal ions (Fe3+, Fe2+, Cu2+, Mn2+) catalyze the autoxidation of 1 by catalytic cycles in which a hydroperoxide intermediate plays key roles. A byproduct of the transition metal-catalyzed oxidation of 1 is superoxide, O2-. Because of its enormous basicity O2- facilitates deprotonation of 1. The C(4)-centered carbanion so produced is oxidized by molecular O2 or by the hydroperoxy radical (HO2) to give radical intermediates and thence 2 and 3. Mechanistic pathways leading to the various products of oxidation of 1 are proposed and the potential roles of oxidation reactions of the indolamine are related to its neurodegenerative properties.
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PMID:Chemical and enzyme-mediated oxidation of the serotonergic neurotoxin 5,7-dihydroxytryptamine: mechanistic insights. 131 96

Peroxidase (EC 1.11.1.7)/H2O2, ceruloplasmin (human type X)/O2, and tyrosinase (EC 1.14.18.1)/O2 all oxidized the indolic neurotransmitter 5-hydroxytryptamine (5-HT) in the physiological pH domain. Peroxidase/H2O2 oxidized 5-HT at pH values down to about 2.5. All oxidation reactions generated complex mixtures of products which included at least one known neurotoxin, tryptamine-4,5-dione. In general, the enzymatic oxidation pathways paralleled the in vitro electrochemical oxidation of 5-HT which has permitted suggestions to be made concerning the probable mechanisms of the enzyme-mediated reactions.
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PMID:Interactions of 5-hydroxytryptamine with oxidative enzymes. 190 Dec 10

Reversed-phase ion-pair chromatography was used to monitor the oxidation of four biogenic amines (adrenaline, noradrenaline, dopamine and 5-hydroxytryptamine) by the copper-containing protein, caeruloplasmin. The methods are reproducible and sufficiently rapid to permit the handling of plasma sample batches. Kinetic parameters obtained using the method are in good agreement with those obtained by more traditional means of enzyme assay. Finally, the results support the view that more than one site on the enzyme, whether binding or oxidative, may be involved in the oxidation of biogenic amines, and the possible implications of this are briefly discussed.
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PMID:Use of high-performance liquid chromatography to study the caeruloplasmin-catalysed oxidation of biogenic amines. I. Single substrate systems. 683 16

A comparative study has been carried out of the oxidation of 5-hydroxytryptamine and related compounds by the oxidase present in the gill plates of Mytilus edulis and of caeruloplasmin, the copper containing oxidase of mammalian plasma. Both preparations oxidized indole derivatives carrying a hydroxyl group in the 4-, 5-, 6-, or 7- position. The oxidation of bufoteni ne was compared with that of its 4- and 6-hydroxy analogues; the 4-hydroxy analogue is psil ocine, a naturally occurring hallucinogenic compound. Bufotenine and the 6-hydroxy analogue were oxidized by both preparations with the formation of brown pigments; psilocine was more rapidly oxidized with the appearance of a blue colour. 4-Hydroxytryptamine and 7-hydroxytryptamine were also oxidized, the former with the formation of a blue compound. The N-1-methyl derivatives of both bufotenine and psilocine were also oxidized. The Mytilus preparation acted also on 4-, 5-, and 7-hydroxytryptophan and on 5-hydroxyindole, none of which was oxidized by caeruloplasmin. The Mytilus enzyme also oxidized 5-hydroxyindoleacetic acid. Paraphenylenediamine, a very good substrate of caeruloplasmin, was much more slowly oxidized by the gill plate enzyme. The evidence suggests that the two enzymes catalyse the same reactions, but that the substrate specificity of the mammalian oxidase is somewhat more restricted. Both enzymes are "hydroxyindole oxidases," not specific for 5-hydroxyindoles alone. Inhibitors of the Mytilus oxidase included inhibitors of copper enzymes but not edetate or carbon monoxide. The action of pig serum on 5-hydroxytryptamine was due to caeruloplasmin and not to amine oxidase.
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PMID:A comparative study of hydroxyindole oxidases. 1910 43