Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.16.3.1 - ferroxidase and Organism(s) Lithobates catesbeianus and UniProt Accession P07798

for references in articles please use BRENDA:EC1.16.3.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Lithobates catesbeianus
UNIPROT: P07798
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Lithobates catesbeianus
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
caeruloplasmin
-
-
-
-
ceruloplasmin
-
-
-
-
ferro:O2 oxidoreductase
-
-
-
-
ferroxidase I
-
-
-
-
ferroxidase, iron II:oxygen oxidoreductase
-
-
-
-
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
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
show the reaction diagram
additional information
?
-
-
formation of the diferric-peroxo (DFP) intermediate and of the ferric-oxo products of the ferroxidase reactions
-
-
?
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
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe(II)
-
the active site within each subunit consists of two inequivalent fivecoordinate ferrous centers that are weakly antiferromagnetically coupled, consistent with a my-1,3 carboxylate bridge. The active site ligand set is unusual and likely includes a terminal water bound to each Fe(II) center. The Fe(II) ions bind to the active sites in a concerted manner, and cooperativity among the sites in each subunit is observed
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture
physiological function
additional information
-
residue Asp140 and previously identified residues Glu57 andGlu136 are essential residues to promote the iron oxidation at the ferroxidase site, but the presence of these three carboxylate moieties in close proximity to the catalytic centers is not essential to achieve binding of the Fe2+ substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild-type cages
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FRI2_LITCT
176
0
20592
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
480000
-
about, gel filtration, wild-type enzyme and mutant E57A/E136A/D140A
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multimer
-
Ftns and Bfrs proteins consist of 24 subunits that form a spherical shell, structure analysis and modeling
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of iron-loaded frog M ferritin determined by flash freezing crystals soaked for different times in iron(II) solutions under aerobic conditions. These structures provide the first X-ray picture of iron(III) products at the ferroxidase site in higher eukaryotes ferritins
purified recombinant iron-free E57A/E136A/D140A ferritin mutant variant, hanging drop vapor diffusion technique, mixing of 0.002 ml of 7 mg/ml protein in 20 mm Tris, pH 7.5, with 0.002 ml of reservoir solution composed of 1.6-2.0m MgCl2 and 0.1m bicine, pH 8.0, and equilibration against 0.6 ml reservoir solution, 8°C, 3–6 days to 10 days, for Fe2+-bound enzyme mutant, 0.1m bis-tris propane buffer at pH 6.5 is used for precipitation, X-ray diffraction structure determination and analysis at 1.50 A resolution, modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E130A
-
site-directed mutagenesis, inactive mutant
E136A
-
site-directed mutagenesis, the mutant enzyme activity is reduced compared to wild-type due to a reduced ability of the variant nanocages to populate the ferroxidase sites Fe1 and Fe2, reduced catalytic activity compared to wild-type
E57A
-
site-directed mutagenesis, the mutant enzyme activity is reduced compared to wild-type due to a reduced ability of the variant nanocages to populate the ferroxidase sites Fe1 and Fe2, reduced catalytic activity compared to wild-type
E57A/E136A
-
site-directed mutagenesis, the mutant enzyme activity is reduced compared to wild-type due to a reduced ability of the variant nanocages to populate the ferroxidase sites Fe1 and Fe2, reduced catalytic activity compared to wild-type
E57A/E136A/D140A
-
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme. In the triple variant, only one Mg2+ ion is bound at the Fe1 site, and the ability of the variant cage to process Fe2+ ions is altered. The mutant shows reduced biomineralization efficiency
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwartz, J.K.; Liu, X.S.; Tosha, T.; Theil, E.C.; Solomon, E.I.
Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites
J. Am. Chem. Soc.
130
9441-9450
2008
Lithobates catesbeianus
Manually annotated by BRENDA team
Bertini, I.; Lalli, D.; Mangani, S.; Pozzi, C.; Rosa, C.; Theil, E.C.; Turano, P.
Structural insights into the ferroxidase site of ferritins from higher eukaryotes
J. Am. Chem. Soc.
134
6169-6176
2012
Lithobates catesbeianus (P07798)
Manually annotated by BRENDA team
Bernacchioni, C.; Pozzi, C.; Di Pisa, F.; Mangani, S.; Turano, P.
Ferroxidase activity in eukaryotic ferritin is controlled by accessory-iron-binding sites in the catalytic cavity
Chemistry
22
16213-16219
2016
Lithobates catesbeianus
Manually annotated by BRENDA team
Ruvinsky, A.; Vakser, I.; Rivera, M.
Local packing modulates diversity of iron pathways and cooperative behavior in eukaryotic and prokaryotic ferritins
J. Chem. Phys.
140
115104
2014
Pseudomonas aeruginosa, Lithobates catesbeianus
Manually annotated by BRENDA team