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Information on EC 1.16.3.1 - ferroxidase and Organism(s) Homo sapiens and UniProt Accession P02794

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     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.3 With oxygen as acceptor
                1.16.3.1 ferroxidase
IUBMB Comments
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P02794
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
ferritin, ceruloplasmin, apoferritin, caeruloplasmin, xanthine oxidoreductase, l-ferritin, hephaestin, bacterioferritin, hp-nap, fet3p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
blue copper oxidase
247
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caeruloplasmin
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ceruloplasmin
Cp115
247
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Cp135
247
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Cp200
247
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ferro-O2-oxidoreductase
247
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ferro:O2 oxidoreductase
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-
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ferroxidase
247
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ferroxidase I
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ferroxidase II
247
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ferroxidase, iron II:oxygen oxidoreductase
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H ferritin
287742
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H-chain ferritin
247
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hephaestin
247
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human ceruloplasmin form I
247
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human H ferritin
287742
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human H-chain ferritin
247
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iron(II): oxygen oxidoreductase
-
-
-
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non-ceruloplasmin ferroxidase
247
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rhHp
247
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rHuHF
247
recombinant human H-chain ferritin
serum ferroxidase
247
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
show the reaction diagram
steady state kinetic analysis, ferroxidase and cuprous oxidase activities are due to the same electron transfer site on the enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
Fe(II):oxygen oxidoreductase
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-37-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-chloro-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-methoxy-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-methyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-nitro-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-sulfonic acid-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
4 Cu+ + 4 H+ + O2
4 Cu2+ + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
show the reaction diagram
-
-
-
-
?
4-methylcatechol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
4-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxyindol-3-ylacetic acid + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptophan + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptophol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
alimemazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
show the reaction diagram
-
-
-
-
?
apotransferrin + Fe2+ + O2
diferric transferrin + H2O
show the reaction diagram
-
-
-
-
?
ascorbate + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
catechol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
chlorpromazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
diethazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
dihydroxyphenylethylamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
durenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
ferrous ammonium sulfate + O2
?
show the reaction diagram
-
-
-
-
?
ferrous ammonium sulfate + O2
? + H2O
show the reaction diagram
-
-
-
-
?
fluphenazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
L-norepinephrine + Fe2+ + O2
?
show the reaction diagram
-
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-
-
?
m-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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-
-
?
N,N'-dimethyl-p-phenylenediamine + Cu2+ + O2
N,N'-dimethyl-p-phenylenediamine radical + Cu+
show the reaction diagram
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-
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?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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-
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?
N,N'-dimethyl-p-phenylenediamine + Fe3+ + O2
?
show the reaction diagram
-
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?
N,N,N',N'-tetramethyl-p-phenylenediamine + Fe2+
?
show the reaction diagram
-
-
-
-
?
N,N-diethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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?
N,N-dimethyl-m-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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?
N,N-dimethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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?
N-(p-methoxyphenyl)-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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-
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?
N-acetyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
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-
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?
N-ethyl-N-(2-hydroxyethyl)-p-phenylenediamine Fe2+ + O2
?
show the reaction diagram
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-
-
?
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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-
-
?
N-phenyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
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-
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?
o-aminophenol + Fe2+ + O2
?
show the reaction diagram
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-
-
?
o-dianisidine + Fe2+ + O2
?
show the reaction diagram
-
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-
-
?
o-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
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-
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?
p-aminophenol + Fe2+ + O2
?
show the reaction diagram
-
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-
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?
p-anisidine + Fe2+ + O2
?
show the reaction diagram
-
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-
-
?
p-phenylenediamine + Cu2+ + O2
p-phenylenediamine radical + Cu+
show the reaction diagram
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
periciazine + Fe2+ + O2
?
show the reaction diagram
-
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-
-
?
perphenazine + Fe2+ + O2
?
show the reaction diagram
-
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-
-
?
prochlorperazine + Fe2+ + O2
?
show the reaction diagram
-
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-
-
?
promazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
prometazine + Fe2+ + O2
?
show the reaction diagram
-
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-
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?
pyrogallol + Fe2+ + O2
?
show the reaction diagram
-
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-
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?
quinone + Fe2+ + O2
?
show the reaction diagram
-
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?
thioridazine + Fe2+ + O2
?
show the reaction diagram
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?
trifluoperazine + Fe2+ + O2
?
show the reaction diagram
-
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-
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?
triflupromazine + Fe2+ + O2
?
show the reaction diagram
-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
additional information
?
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treatment of mouse BV-2 cells and primary microglial cells with ceruloplasmin induces nitric oxide release and inducible NO synthase mRNA expression. Presence of ceruloplasmin increases levels of mRNAs encoding tumor necrosis factor-alpha, interleukin-1beta, cyclooxygenase-2, and NADPH oxidase. Treatment of BV-2 cells and primary microglia with ceruloplasmin induces phosphorylation of p38 MAP kinase. Ceruloplasmin induces nuclear factor kappaB activation, showing a more sustained pattern than seen with bacterial lipopolysaccharide. Ceruloplasmin-stimulated NO induction is significantly attenuated by p38 inhibitor, SB203580, and the nucleare factor kappaB inhibitor SN50. Ceruloplasmin induces secretion of tumor necrosis factor-alpha and prostaglandin E2 in primary microglial cultures
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
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3.1 atoms per protein molecule
Cr3+
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0.1 M, activity 102%
Iron
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ceruloplasmin is regulated by cellular iron status
Ni2+
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activating
Zn2+
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activating
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-aminohexanoic acid
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Ba2+
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weak inhibitor
Ca2+
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weak inhibitor
Cr3+
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strong inhibitor
K+
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weak inhibitor
Li+
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weak inhibitor
N3-
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anion behaves as an inhibitor of the oxidase activity versus Fe2+
Na+
-
weak inhibitor
Sn2+
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weak inhibitor
Sodium azide
Zn2+
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2 M Zn2+ occupies the ferroxidase center as redox-invariant analogue of Fe2+
ZrO2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lactoferrin
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apolactoferrin increases the oxidation rate of Fe(II) by ceruloplasmin 1.25fold at pH 5.5. Lactoferrin saturated with Fe3+ or Cu2+ increases the oxidation rate of Fe2+ 1.6fold when in 1:1 ratio with enzyme
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pyrrolidine dithiocarbamate
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regulation of ceruloplasmin expression by a copper-dependent transcriptional mechanism