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Information on EC 1.16.3.1 - ferroxidase

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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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UNIPROT: Q99YU7
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Word Map
The enzyme appears in 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
Dpr
DNA-binding protein from starved cells
caeruloplasmin
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ceruloplasmin
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ferro:O2 oxidoreductase
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ferroxidase I
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ferroxidase, iron II:oxygen oxidoreductase
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iron(II): oxygen oxidoreductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
binding and oxidization of iron, thus preventing the formation of harmful reactive oxygen species
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
bending magnet macromolecular crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of the crystal structure of Streptococcus pyogenes Dpr in iron-free and iron-bound form at 2.0 and 1.93 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D66A
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
D77A
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
E81A
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
H50A
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
H62A
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haikarainen, T.; Tsou, C.C.; Wu, J.J.; Papageorgiou, A.C.
Crystal structures of Streptococcus pyogenes Dpr reveal a dodecameric iron-binding protein with a ferroxidase site
J. Biol. Inorg. Chem.
15
183-194
2010
Streptococcus pyogenes (Q99YU7), Streptococcus pyogenes
Manually annotated by BRENDA team