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Information on EC 1.16.3.1 - ferroxidase and Organism(s) Mus musculus and UniProt Accession Q61147

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EC Tree
     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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This record set is specific for:
Mus musculus
UNIPROT: Q61147
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ferritin, ceruloplasmin, ferroxidase, apoferritin, xanthine oxidoreductase, caeruloplasmin, l-ferritin, hephaestin, bacterioferritin, hp-nap, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferroxidase
-
mouse ceruloplasmin
ceruloplasmin with ferroxidase activity detected by native PAGE
caeruloplasmin
-
-
-
-
ceruloplasmin
-
-
-
-
ferritin
-
-
ferro:O2 oxidoreductase
-
-
-
-
ferroxidase I
-
-
-
-
ferroxidase, iron II:oxygen oxidoreductase
-
-
-
-
hephaestin
-
-
iron(II): oxygen oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
apotransferrin + Fe2+
holotransferrin + ?
show the reaction diagram
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
-
developmental role of enzyme in nervous system organization
-
-
?
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
additional information
?
-
-
developmental role of enzyme in nervous system organization
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sodium azide
1-2.5 mM sodium azide reduces ferroxidase activity markedly
Bathocuproine disulfonate
-
incubation of C6 glioma cells with the copper chelator bathocuproine disulfonate prevents expression of ceruloplasmin on the cell surface and leads to a decrease in cellular ceruloplasmin. Incubation of cells with bathocuproine disulfonate also reduces the ability of cells to lower their ferritin levels
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CuCl2
-
increase in enzyme mRNA due to transcriptional activation of enzyme gene’s promoter
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.25
in an Erel assay measuring loss of Fe2+
0.3
in a transferrin assay measuring transformation of apotransferrin to holotransferrin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and ceruloplasmin knockout mice
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
intestinal enterocyte
Manually annotated by BRENDA team
-
both hypoxia and CuCl2 increase ceruloplasmin mRNA levels in hepatoma cells due to transcriptional induction of enzyme gene promoter
Manually annotated by BRENDA team
-
mouse embryonal carcinoma cell line, addition of enzyme to culture medium induces aggregation within 24 h, with half-maximal effect at 0.05 mM. No association with apoptosis, necrosis or changes in secretory function. aggregation is less pronounce in aging neurons, K+ channels seem not to be involved
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CERU_MOUSE
1061
0
121151
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
transfection of C6 glioma cells with RNAi oligonucleotide pools specific for cell suface GPI-ceruloplasmin leads to decreased levels of GPI-ceruloplasmin but does not affect accumulation of ferritin, when cells are incubated with iron. In the absence of ceruloplasmin, the transporter protein ferroportin is rapidly internalized and degraded. Depeltion of extra-cellular Fe(II) can maintain cell surface ferroportin in the absence of ceruloplasmin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
blood plasma ceruloplasmin was purified by DEAE-Sepharose chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in C6 glioma cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maltais, D.; Desroches, D.; Aouffen, M.; Mateescu, M.A.; Wang, R.; Paquin, J.
The blue copper ceruloplasmin induces aggregation of newly differentiated neurons: a potential modulator of nervous system organization
Neuroscience
121
73-82
2003
Mus musculus
Manually annotated by BRENDA team
Martin, F.; Linden, T.; Katschinski, D.M.; Oehme, F.; Flamme, I.; Mukhopadhyay, C.K.; Eckhardt, K.; Troeger, J.; Barth, S.; Camenisch, G.; Wenger, R.H.
Copper-dependent activation of hypoxia-inducible factor (HIF)-1: implications for ceruloplasmin regulation
Blood
105
4613-4619
2005
Mus musculus
Manually annotated by BRENDA team
De Domenico, I.; Ward, D.M.; di Patti, M.C.; Jeong, S.Y.; David, S.; Musci, G.; Kaplan, J.
Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
EMBO J.
26
2823-2831
2007
Mus musculus
Manually annotated by BRENDA team
Gray, L.W.; Kidane, T.Z.; Nguyen, A.; Akagi, S.; Petrasek, K.; Chu, Y.L.; Cabrera, A.; Kantardjieff, K.; Mason, A.Z.; Linder, M.C.
Copper proteins and ferroxidases in human plasma and that of wild-type and ceruloplasmin knockout mice
Biochem. J.
419
237-245
2009
Rattus norvegicus, Homo sapiens (P00450), Homo sapiens, Mus musculus (Q61147), Mus musculus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Chen, H.; Attieh, Z.K.; Gao, H.; Huang, G.; Su, T.; Ke, W.; Vulpe, C.D.
Age-related changes in iron homeostasis in mouse ferroxidase mutants
Biometals
22
827-834
2009
Mus musculus
Manually annotated by BRENDA team