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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: O29424
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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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O29424_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
173
0
20316
TrEMBL
Secretory Pathway (Reliability: 4)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the ferritin at 2.1 and 2.7 A resolution for the native and iron bound proteins, respectively. X-ray crystallographic data indicate that the metal ion binding mode, secondary and tertiary structure of the enzyme closely resemble those of bacterial and eukaryotic H-type ferritins. However, the tetrahedral quarternary structure of the enzyme is unprecedented in its symmetry and in the presence of four large pores in the ferritin shell
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, E.; Cascio, D.; Sawaya, M.R.; Gingery, M.; Schrder, I.
Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus
Structure
13
637-648
2005
Archaeoglobus fulgidus (O29424), Archaeoglobus fulgidus
Manually annotated by BRENDA team