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2-chloro-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-methoxy-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-methyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-nitro-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-sulfonic acid-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
3,4-dihydroxyphenethylamine + Fe2+ + O2
?
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
4 Mn(II) + 4 H+ + O2
4 Mn(III) + 2 H2O
-
-
-
-
?
4 Mn(III) + 4 H+ + O2
4 Mn(IV) + 2 H2O
-
-
-
-
?
4-methylcatechol + Fe2+ + O2
?
-
-
-
-
?
4-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
5-hydroxyindol-3-ylacetic acid + Fe2+ + O2
?
-
-
-
-
?
5-hydroxytryptamine + Fe2+ + O2
?
-
-
-
-
?
5-hydroxytryptophan + Fe2+ + O2
?
-
-
-
-
?
5-hydroxytryptophol + Fe2+ + O2
?
-
-
-
-
?
alimemazine + Fe2+ + O2
?
-
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
apotransferrin + Fe2+ + O2
diferric transferrin + H2O
-
-
-
-
?
catechol + O2
?
-
mushroom tyrosinase is able to catalyse the oxidation of Fe2+ to Fe3+
-
-
?
chlorpromazine + Fe2+ + O2
?
-
-
-
-
?
diethazine + Fe2+ + O2
?
-
-
-
-
?
durenediamine + Fe2+ + O2
?
-
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
Fe(II) + H+ + O2
Fe(III) + H2O
Fe(II) + hydroquinone + O2
Fe(III) + ? + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
ferrous ammonium sulfate + O2
?
-
-
-
-
?
ferrous ammonium sulfate + O2
? + H2O
-
-
-
-
?
fluphenazine + Fe2+ + O2
?
-
-
-
-
?
hydroquinone + Fe2+ + O2
?
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
L-norepinephrine + Fe2+ + O2
?
-
-
-
-
?
m-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
monophenol + O2
catechol + H2O
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
N,N,N',N'-tetramethyl-p-phenylenediamine + Fe2+
?
-
-
-
-
?
N,N-diethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N,N-dimethyl-m-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N-(p-methoxyphenyl)-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N-acetyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N-ethyl-N-(2-hydroxyethyl)-p-phenylenediamine Fe2+ + O2
?
-
-
-
-
?
N-ethyl-N-(2-hydroxyethyl)p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
r
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N-phenyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
NADH + O2
NAD+ + H2O
-
-
-
-
?
o-aminophenol + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
o-phenylenediamine + Fe2+ + O2
?
p-aminophenol + Fe2+ + O2
?
-
-
-
-
?
p-anisidine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
periciazine + Fe2+ + O2
?
-
-
-
-
?
perphenazine + Fe2+ + O2
?
-
-
-
-
?
prochlorperazine + Fe2+ + O2
?
-
-
-
-
?
promazine + Fe2+ + O2
?
-
-
-
-
?
prometazine + Fe2+ + O2
?
-
-
-
-
?
pyrogallol + Fe2+ + O2
?
-
-
-
-
?
quinone + Fe2+ + O2
?
-
-
-
-
?
thioridazine + Fe2+ + O2
?
-
-
-
-
?
trifluoperazine + Fe2+ + O2
?
-
-
-
-
?
triflupromazine + Fe2+ + O2
?
-
-
-
-
?
additional information
?
-
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
similar kinetic activity towards Cu+ as substrate
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the stoichiometry of Fe(II), ferroxldase, and oxygen is 4:1:1
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
two Fe2+ ions occupy sites Fe1 and Fe2 in the ferroxidase cavity, structure overview
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
similar kinetic activity towards Cu+ as substrate. The ferroxidase and cuprous oxidase activities are due to the same electron transfer site on the enzyme
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
similar kinetic activity towards Cu+ as substrate. The ferroxidase and cuprous oxidase activities are due to the same electron transfer site on the enzyme
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
Thermosynechococcus vestitus
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
-
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
-
-
-
-
?
ascorbate + Fe2+ + O2
?
-
-
-
-
?
ascorbate + Fe2+ + O2
?
-
-
-
-
?
catechol + Fe2+ + O2
?
-
-
-
-
?
catechol + Fe2+ + O2
?
-
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
-
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
-
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
kinetic studies and determination of rate constants at various steps
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
437996, 437997, 437998, 438000, 438001, 438002, 438003, 438004, 438005, 438006, 438007, 438008, 438009, 438010, 438011, 438012, 438013, 438014, 438015, 438016, 438017, 438020, 438021, 438022, 438024, 438026, 438027, 438028, 438029, 438030, 438032 -
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
multicopper oxidase essential for normal iron homeostasis
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
iron acquisition pathway
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
-
-
-
-
?
o-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
o-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
no p-phenylenediamine oxidase activity by ferroxidase II
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
additional information
?
-
AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid
-
-
?
additional information
?
-
-
AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid
-
-
?
additional information
?
-
AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid
-
-
?
additional information
?
-
-
possesses superoxide dismutase activity
-
-
?
additional information
?
-
-
Mn oxidation from soluble Mn(II) to Mn(IV) oxides is a two-step reaction catalyzed by an MCO-containing complex
-
-
?
additional information
?
-
-
possesses superoxide dismutase activity
-
-
?
additional information
?
-
-
the Fe-uptake proteins Fet31 and Fet34 support a mechanism of Fe-trafficking that involves channelling of the CaFet34-generated Fe3+ directly to CaFtr1 for transport into the cytoplasm
-
-
?
additional information
?
-
-
enzymatic activity of sFet34 towards ferrous iron is determined by quantifying the velocity of O2 uptake using standard O2-electrode protocols
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
only ceruloplasmin capable of complete reoxidation by oxygen
-
-
?
additional information
?
-
-
the non-heme iron-containing ferritin has dual ferroxidase and DNA-binding activities, overview
-
-
?
additional information
?
-
-
the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity
-
-
?
additional information
?
-
-
the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
multifunctional protein, copper transport, molecule directly involved in iron mobilization to the plasma by means of its ferroxidase activity, regulator of circulating biogenic amine levels through its oxidase activity
-
-
?
additional information
?
-
-
caeruloplasmin inhibits lipid peroxidation and deoxyribose degradation stimulated by iron and copper salts
-
-
?
additional information
?
-
-
ferroxidase II does not catalyze the oxidation of benzylamine
-
-
?
additional information
?
-
-
possesses superoxide dismutase activity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
enzyme metal binding structure, overview
-
-
?
additional information
?
-
-
enzyme metal binding structure, overview
-
-
?
additional information
?
-
-
development of the classic chromophoric complex FeIIHx(Tar)2 (H2Tar), 4-(2-thiazolylazo)-resorcinol (x = 0-2) as a robust substrate for evaluation of the ferroxidase function of ceruloplasmin and related enzymes. The catalysis can be followed conveniently in real-time by monitoring the solution absorbance at 720 nm, a fingerprint of FeIIHx(Tar)2. The complex is oxidized to its ferric form FeIIIHx(Tar)2. Fe(II) is transferred formally from FeIIHx(Tar)2 to the substrate docking/oxidation (SDO) site(s) in ceruloplasmin, followed by oxidation to product Fe(III) that is trapped again by the ligand. Each Tar ligand in the above bis-complex coordinates the metal center in a meridional tridentate mode involving a pH-sensitive -OH group (pKa >12), and this imposes rapid Fe(II) and Fe(III) transfer kinetics to facilitate the catalytic process. Method evaluation and proposed mechanism, detailed overview
-
-
?
additional information
?
-
-
usage of a kinetic, automated assay to determine the ferroxidase activity of ceruloplasmin. Enzyme ceruloplasmin shows oxidase activity against ferrous ion,which is the natural substrate, as well as polyphenols, and polyamines. The enzyme oxidizes p-phenylenediamine and o-dianisidine, the substrates are used for assay optimization and evaluation, overview
-
-
?
additional information
?
-
-
enzyme is involved in conferring peroxide tolerance to the bacterium
-
-
?
additional information
?
-
-
formation of the diferric-peroxo (DFP) intermediate and of the ferric-oxo products of the ferroxidase reactions
-
-
?
additional information
?
-
-
developmental role of enzyme in nervous system organization
-
-
?
additional information
?
-
-
competitive binding with Zn2+
-
-
?
additional information
?
-
both in vitro and in vivo ceruloplasmin is able to form the specific complex with lactoferrin, the cationic transferrin of exocrine secretions and secretory granules of neutrophils
-
-
?
additional information
?
-
both in vitro and in vivo ceruloplasmin is able to form the specific complex with lactoferrin, the cationic transferrin of exocrine secretions and secretory granules of neutrophils
-
-
?
additional information
?
-
-
Fet3p is able to catalyze effectively the incorporation of iron onto apotransferrin
-
-
?
additional information
?
-
-
Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface
-
-
?
additional information
?
-
-
Dpr is also able to bind zinc as an oxidation stable replacement for iron, metal complex binding structure, formation of a di-zinc center, a third zinc ion is found on the surface of the protein, overview
-
-
?
additional information
?
-
-
the divalent metal ions Zn2+, Mn2+, Ni2+, Co2+, and Cu2+ all bind to the ferroxidase center similarly to Fe2+, with moderate affinity, while Mg2+ does not. SsDpr is able to bind various metals as substitutes for iron, enzyme-metal complex structure, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
ascorbate oxidase EC 1.10.3.3 activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
-
enzyme HP-NAP belongs to the DNA-protecting proteins under starved conditions (Dps) family, which has significant structural similarities to the dodecameric ferritin family. The overall structure of HP-NAP YS39 is similar to those of other HP-NAPs and Dps proteins
evolution
in addition to the classical classification, another cluster containing AaMco1 and filamentous ascomycete hypothetical proteins, putative multicopper oxidases (MCOs) or proteins called ascorbate oxidases is identified on the basis of sequence similarity. This group is named ascomycete MCOs. Neighbor joining tree of multicopper oxidase amino acid sequences, phylogenetic analysis, overview
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
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
evolution
-
enzyme HP-NAP belongs to the DNA-protecting proteins under starved conditions (Dps) family, which has significant structural similarities to the dodecameric ferritin family. The overall structure of HP-NAP YS39 is similar to those of other HP-NAPs and Dps proteins
-
evolution
-
in addition to the classical classification, another cluster containing AaMco1 and filamentous ascomycete hypothetical proteins, putative multicopper oxidases (MCOs) or proteins called ascorbate oxidases is identified on the basis of sequence similarity. This group is named ascomycete MCOs. Neighbor joining tree of multicopper oxidase amino acid sequences, phylogenetic analysis, overview
-
malfunction
-
cytosolic FOX activity increases 30% in iron-deficient rats (compared with controls) but is unchanged in copper-deficient rats
malfunction
-
knockdown of MCO1 is correlated with increased longevity on high-iron food and decreased iron accumulation
malfunction
strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin ferroxidase activity. The deficiency of ceruloplasmin ferroxidase activity in Ag-fed rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apolactoferrin (apo-LF) is administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron are restored more rapidly than in the control animals. Saturation of apo-LF with iron, provided by active ceruloplasmin, can strongly affect its protective capacity. Phenotype, overview
malfunction
deletion of the rv0846c gene increases the susceptibility of Mycobacterium tuberculosis to copper at least 10fold
malfunction
-
deletion of the rv0846c gene increases the susceptibility of Mycobacterium tuberculosis to copper at least 10fold
-
malfunction
-
strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin ferroxidase activity. The deficiency of ceruloplasmin ferroxidase activity in Ag-fed rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apolactoferrin (apo-LF) is administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron are restored more rapidly than in the control animals. Saturation of apo-LF with iron, provided by active ceruloplasmin, can strongly affect its protective capacity. Phenotype, overview
-
metabolism
the initial step in the iron store mechanism occurs when the Fe(II) is oxidize to Fe(III) at the ferroxidase center (FC) found in the H-chain from mammalian ferritins, bacterial ferritins and Bfr subunits
metabolism
-
the initial step in the iron store mechanism occurs when the Fe(II) is oxidize to Fe(III) at the ferroxidase center (FC) found in the H-chain from mammalian ferritins, bacterial ferritins and Bfr subunits
-
physiological function
binding and oxidization of iron, thus preventing the formation of harmful reactive oxygen species
physiological function
essential to iron homeostasis in green algae
physiological function
-
FOX1 is important for iron uptake in a situation of iron deficiency
physiological function
-
iron provoked inhibition of osteoblast activity leading to osteoporosis and osteopenia is mediated by ferritin and its ferroxidase activity
physiological function
-
stores iron as a hydrous ferric oxide mineral core within a shell-like structure of 4/3/2 octahedral symmetry
physiological function
-
Dps proteins contain a ferroxidase site that binds and oxidizes iron, thereby consuming H2O2 and preventing hydroxyl radical formation by Fenton reaction. Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface
physiological function
Thermosynechococcus vestitus
DpsA-Te can protect DNA molecules against Fe(II)-mediated and H2O2-mediated damage. Dps-Te and DpsA-Te, together with ferritin, play an important role in alleviating the toxic effects of reactive oxygen species, physiological basis of the coexistence of two Dps proteins in the organism, overview
physiological function
-
ferritin is a ubiquitous iron-storage protein that has 24 subunits. Each subunit of ferritins that exhibit high Fe2+ oxidation rates has a diiron binding site, the socalled ferroxidase center. The role of the ferroxidase center appears to be essential for the iron-oxidation catalysis of ferritins
physiological function
-
native function includes the interaction with the iron permease, Ftr1p, and wild-type high-affinity iron uptake activity. The four essential sequons are found within relatively nonpolar regions located in surface recesses and are strongly conserved among fungal Fet3 proteins
physiological function
-
the non-heme iron-binding ferritin with dual ferroxidase and DNA-binding functionality reported herein, may play a significant urease-independent role in the acid adaptation of Helicobacter pylori under physiological conditions in vivo
physiological function
-
the two ferroxidases are likely involved in high-affinity Fe-uptake in Candida albicans, Fet31 and Fet34, both support Fe-uptake along with an Ftr1 protein, either from Candida albicans or from Saccharomyces cerevisiae. CaFtr1 and not CaFtr2 is required for the virulence of the pathogen
physiological function
-
ceruloplasmin is one of the most complex multicopper oxidase enzymes and plays an essential role in the metabolism of iron in mammals. Ferrous ion supplied by the ferroportin exporter is converted by ceruloplasmin to ferric ion that is accepted by plasma metallo-chaperone transferrin. The multicopper oxidase enzymes mediate transfer of the iron from the cell export pump ferroportin to the plasma metallo-chaperone transferrin. Specifically, they are responsible for conversion of Fe(II) to Fe(III), the form in which it is transported in the blood by transferrin
physiological function
-
ceruloplasmin's primary physiological role in the association of plasma redox reactions
physiological function
-
ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in Bfrs. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
-
ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in bacterial Ftn. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
-
ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in the heavy (H)-type and M-type subunits of eukaryotic Ftns. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
-
ferritins are iron-storage nanocage proteins that catalyze the oxidation of Fe2+ to Fe3+ at ferroxidase sites. Ferroxidase activity in eukaryotic ferritin is controlled by accessory-iron-binding sites in the catalytic cavity, a ferroxidase-active cage, overview
physiological function
-
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
-
neutrophil-activating protein (HP-NAP) is one of a number of virulence factors in Helicobacter pylori. The enzyme promote the adhesion of neutrophils to endothelial cells, and activates NADPH oxidase to produce reactive oxygen species via a cascade of intracellular activation events. HP-NAP binds to the outer membrane surface, which mediates binding to mucin or glycosphingolipids. This protein can also stimulate the production of tissue factor and plasminogen activator inhibitor-2 by human monocytes. HP-NAP can cross the endothelium to promote neutrophil adhesion in vivo and can activate the underlying mast cells. HP-NAP stimulates Th1 immune responses by inducing the production of cytokines, such as interleukin-12 (IL-12) and IL-23. HP-NAP is a major antigen in the immune response to Helicobacter pylori infections. HP-NAP protects Helicobacter pylori from iron-mediated oxidative DNA damage by sequestering free iron, similar to Dps proteins, which protect DNA from oxidative damage
physiological function
the recombinant Chlorobium tepidum ferritin (rCtFtn) is able to oxidize iron with a moderate ferroxidase activity
physiological function
multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
physiological function
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
physiological function
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
physiological function
-
neutrophil-activating protein (HP-NAP) is one of a number of virulence factors in Helicobacter pylori. The enzyme promote the adhesion of neutrophils to endothelial cells, and activates NADPH oxidase to produce reactive oxygen species via a cascade of intracellular activation events. HP-NAP binds to the outer membrane surface, which mediates binding to mucin or glycosphingolipids. This protein can also stimulate the production of tissue factor and plasminogen activator inhibitor-2 by human monocytes. HP-NAP can cross the endothelium to promote neutrophil adhesion in vivo and can activate the underlying mast cells. HP-NAP stimulates Th1 immune responses by inducing the production of cytokines, such as interleukin-12 (IL-12) and IL-23. HP-NAP is a major antigen in the immune response to Helicobacter pylori infections. HP-NAP protects Helicobacter pylori from iron-mediated oxidative DNA damage by sequestering free iron, similar to Dps proteins, which protect DNA from oxidative damage
-
physiological function
-
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
-
physiological function
-
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
-
physiological function
-
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
-
physiological function
-
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
physiological function
-
multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
-
physiological function
-
FOX1 is important for iron uptake in a situation of iron deficiency
-
physiological function
-
the recombinant Chlorobium tepidum ferritin (rCtFtn) is able to oxidize iron with a moderate ferroxidase activity
-
physiological function
-
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
-
additional information
-
core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum. Fet3 protein lacking any one of the glycan units is found in an intracellular high-molecular mass species. But the missing carbohydrate is not required for native structure and biologic activity
additional information
-
Dps-like, i.e. DNA-binding protein from starved cells-like, proteins belong to the ferritin superfamily. They form 12-mers instead of 24-mers, in contrast to ferritins, and have a different ferroxidase center, and are able to store a smaller amount of about 500 iron atoms in a hollow cavity
additional information
Thermosynechococcus vestitus
DpsA-Te ows a unique substitution of a metal ligand at the A-site, i.e. His78 in place of the canonical Asp, and a His164 in place of a hydrophobic residue at a metal-coordinating distance in the B-site. In contrast to the typical behavior of Dps proteins, where Fe2+ oxidation by H2O2 is about 100fold faster than by O2, in DpsA-Te the ferroxidation efficiency of O2 is very high and resembles that of H2O2. DpsA-Te contains two Zn2+ bound at the ferroxidase center. The latter Zn2+ is displaced by incoming iron, such that Zn(II)-Fe(III) complexes are formed upon oxidation
additional information
ferritin is a ubiquitous iron storage protein that possesses ferroxidase activity
additional information
-
ferritin is a ubiquitous iron storage protein that possesses ferroxidase activity
additional information
-
protein localization patterns and metal-enzyme complexes of Candida albicans wild-type and mutant enzymes compared to Saccharomyces cerevisiae enzymes, overview
additional information
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structure of the diiron binding site of ferritin, overview
additional information
-
the organism contains a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities, that is upregulate under acid stress, overview. By its binding to DNA under acid stress, HP-ferritin is able to protect DNA from oxidative damage caused by free radicals in the presence of metal ions such as iron and copper, overview
additional information
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Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview
additional information
Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview. Vibrio cholerae Dps (VcDps) and DpsA representing type I and II channels
additional information
encapsulin A is comprising 180 virus-like structural proteins with an outer diameter of 32 nm. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
encapsulin is comprising 60 virus-like structural proteins with an outer diameter of 24 nm. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
in the dodecameric Dps, translocation position T3 is located at the channel exit where conserved Asp residues narrow the pore diameter significantly, forming a scaffold for tethering ions at the inner wall of the protein. After crossing the constriction zone, three ferroxidase centers are located about 20 A apart and iron can move along negatively charged residues at the inner wall towards the ferroxidase center with high-affinity binding. Mechanism for ferroxidase-mediated biomineralization, overview
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
additional information
-
residues His25, His37, Asp52, and Glu56 are perfectly conserved among HP-NAPs, dodecameric ferritin, and Dps proteins, and play important roles in metal-ion binding
additional information
the dodecameric Dps protein with an outer particle radius of 8 nm and a storage capacity of about 500 iron atoms. Ferritin can be assembled using six tetramers per cubic face, while Dps complexes are formed through the assembly of six protein dimers on each plane of the cube. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits
additional information
-
the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits
additional information
-
residues His25, His37, Asp52, and Glu56 are perfectly conserved among HP-NAPs, dodecameric ferritin, and Dps proteins, and play important roles in metal-ion binding
-
additional information
-
Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview. Vibrio cholerae Dps (VcDps) and DpsA representing type I and II channels
-
additional information
-
encapsulin A is comprising 180 virus-like structural proteins with an outer diameter of 32 nm. Mechanism for ferroxidase-mediated biomineralization, overview
-
additional information
-
in the dodecameric Dps, translocation position T3 is located at the channel exit where conserved Asp residues narrow the pore diameter significantly, forming a scaffold for tethering ions at the inner wall of the protein. After crossing the constriction zone, three ferroxidase centers are located about 20 A apart and iron can move along negatively charged residues at the inner wall towards the ferroxidase center with high-affinity binding. Mechanism for ferroxidase-mediated biomineralization, overview
-
additional information
-
the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits
-
additional information
-
the dodecameric Dps protein with an outer particle radius of 8 nm and a storage capacity of about 500 iron atoms. Ferritin can be assembled using six tetramers per cubic face, while Dps complexes are formed through the assembly of six protein dimers on each plane of the cube. Mechanism for ferroxidase-mediated biomineralization, overview
-
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E184A
-
a Fet34 mutant, that shows altered kinetics compared to the wild-type enzyme
E184A/D408A
-
a Fet34 mutant, that shows altered kinetics compared to the wild-type enzyme
R454A
-
Arg454 is mutated to Ala in order to reduce proteolytic cleavage
C500S
mutation leads to loss of the T1 copper
M358S/M361S/M362S/M364S/M366S
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
W133F
protein is lesser sensitive to Fe2+ than wild-type protein
W35F
fluorescence spectrum is blunted compared to wild-type protein
W35F/W133F
oxidation of Fe2+ to Fe3+ is slightly reduced
C500S
-
mutation leads to loss of the T1 copper
-
M358S/M361S/M362S/M364S/M366S
-
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
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D616A/H621A/E960A/H965A
-
iron binding sites are mutated but one is unaffected. Km and kcat for substrate 4-phenylenediamine decreased compared to wild-type. kcat (Fe2+) up to 10fold decreased compared to wild-type. Mutant does not retain a high-affinity iron oxidation component
E140A
site-directed mutagenesis, the initial velocity of iron oxidization is reduced in the mutant
E140Q
site-directed mutagenesis, the initial velocity of iron oxidization is highly reduced in the mutant. The side chain of the mutated Gln140 is fixed by a hydrogen bond, whereas that of native Glu140 is flexible
E264A/H269A/D616A/H621A
-
iron binding sites are mutated but one is unaffected. Km and kcat for substrate 4-phenylenediamine decreased compared to wild-type. Km for high-affinity oxidation of Fe2+ decreased compared to wild-type. kcat (Fe2+) up to 10fold decreased compared to wild-type. Only mutant that retains a high-affinity iron oxidation component
E264A/H269A/D616A/H621A/E960A/H965A
-
all three iron binding sites are mutated. Km and kcat for substrate 4-phenylenediamine decreased compared to wild-type. kcat (Fe2+) up to 75 fold decreased compared to wild-type. Mutant does not retain a high-affinity iron oxidation component
E264A/H269A/E960A/H965A
-
iron binding sites are mutated but one is unaffected. Km and kcat for substrate 4-phenylenediamine decreased compared to wild-type. kcat (Fe2+) up to 10fold decreased compared to wild-type. Mutant does not retain a high-affinity iron oxidation component
K86Q
-
equivalent to wild-type
K86Q/E107D
-
reduced reduction activity
K86Q/E27D
-
in X-ray absorption same properties as wild-type, but reduced reduction activity
K86Q/E27D/E107D
-
no reduction activity
W93F/Y34W
-
no alteration in the rate of Fe2+ oxidation
W93F/Y34W/Y29Q
-
no alteration in the rate of Fe2+ oxidation
Y34W/W93F/D131I/E134F
-
no transport of Fe2+ to the ferroxidase center
H31G
-
significant decrease in binding affinity of Fe(II), no altring of the binding stoichiometry. Mutation has little effect on the kinetics of iron uptake and the formation of micelles inside the protein shell
H31G/H43G
-
no measurable affinity for binding of Fe(II). Mutation has little effect on the kinetics of iron uptake and the formation of micelles inside the protein shell
H31G/H43G/D58A
-
no measurable affinity for binding of Fe(II). Mutation has little effect on the kinetics of iron uptake and the formation of micelles inside the protein shell
H43G
-
significant decrease in binding affinity of Fe(II), no altring of the binding stoichiometry. Mutation has little effect on the kinetics of iron uptake and the formation of micelles inside the protein shell
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
C35A
putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity
C486A
cysteine 486 is required for MmcO activity. Mutation results in inactive Rv0846c protein which does not protect Mycobacterium tuberculosis against copper stress
C35A
-
putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity
-
C486A
-
cysteine 486 is required for MmcO activity. Mutation results in inactive Rv0846c protein which does not protect Mycobacterium tuberculosis against copper stress
-
D278A
-
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type, in crease in Km-value compared to wild-type
E185A/Y354A
-
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type, in crease in Km-value compared to wild-type
N113A
-
site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics, but steady-state localization in the plasma membrane like the wild-type enzyme
N194A
-
site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics
N198A
-
site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics
N244A
-
site-directed mutagenesis of a potential N-glycosylation site
N265A
-
site-directed mutagenesis of a potential N-glycosylation site
N27A
-
site-directed mutagenesis of a potential N-glycosylation site
N292A
-
site-directed mutagenesis of a potential N-glycosylation site
N300A
-
site-directed mutagenesis of a potential N-glycosylation site
N359A
-
site-directed mutagenesis of a potential N-glycosylation site
N381A
-
site-directed mutagenesis of a potential N-glycosylation site
N74A
-
site-directed mutagenesis of a potential N-glycosylation site
N77A
-
site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics, but steady-state localization in the plasma membrane like the wild-type enzyme
N88A
-
site-directed mutagenesis of a potential N-glycosylation site
T307A
-
site-directed mutagenesis of a potential O-glycosylation site
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
D47A
-
interactions of mutant D74A with various divalent ions compared to the wild-type enzyme, overview
A19Y
site-directed mutagenesis, introduction of a stop codon at position 166 and replacment of Ala19 by a Tyr residue. The mutant is able to bind, oxidize and store iron, and its activity is inhibited by Zn(II) as described for other ferritins. The mutant enzymes shows reduced activity and protein stability compared to the wild-type enzyme
A19Y
-
site-directed mutagenesis, introduction of a stop codon at position 166 and replacment of Ala19 by a Tyr residue. The mutant is able to bind, oxidize and store iron, and its activity is inhibited by Zn(II) as described for other ferritins. The mutant enzymes shows reduced activity and protein stability compared to the wild-type enzyme
-
D283A
-
wild-type reduction potential
D283A
-
X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 7-fold increase in Km value for Fe(II)
D409A
-
increase in reduction potential by 120 mV
D409A
-
X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 4-fold increase in Km value for Fe(II)
E185A
-
CD and MCD spectra similar to wild-type
E185A
-
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type, in crease in Km-value compared to wild-type, inactive in support of iron uptake
E185A
-
wild-type reduction potential
E185A
-
X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 4-fold increase in Km value for Fe(II)
E185A/D409A
-
increase in reduction potential by 120 mV, complete loss of specificity for Fe(II), functions kinetically as an inefficient laccase
E185A/D409A
-
X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 800-fold increase in Km value for Fe(II)
E185D
-
2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type
E185D
-
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type
Y354A
-
2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type
Y354A
-
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type, in crease in Km-value compared to wild-type
Y354F
-
CD and MCD spectra similar to wild-type
Y354F
-
normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type
additional information
construction of a truncated enzyme mutant by deletion of the first 83 amino acids containing the putative N-terminal transmembrane helix in order to obtain a soluble protein. Expression of the DELTA-N-truncated protein leads to the production of an insoluble protein that presents a molecular weight estimated at 75 kDa. The truncated protein loses the N-terminal His-tag during or after renaturation step but retains to keep the expected molecular weight, the truncated enzyme shows slightly reduced activity compared to wild-type
additional information
-
construction of a truncated enzyme mutant by deletion of the first 83 amino acids containing the putative N-terminal transmembrane helix in order to obtain a soluble protein. Expression of the DELTA-N-truncated protein leads to the production of an insoluble protein that presents a molecular weight estimated at 75 kDa. The truncated protein loses the N-terminal His-tag during or after renaturation step but retains to keep the expected molecular weight, the truncated enzyme shows slightly reduced activity compared to wild-type
additional information
-
construction of a truncated enzyme mutant by deletion of the first 83 amino acids containing the putative N-terminal transmembrane helix in order to obtain a soluble protein. Expression of the DELTA-N-truncated protein leads to the production of an insoluble protein that presents a molecular weight estimated at 75 kDa. The truncated protein loses the N-terminal His-tag during or after renaturation step but retains to keep the expected molecular weight, the truncated enzyme shows slightly reduced activity compared to wild-type
-
additional information
deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability
additional information
-
deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability
additional information
-
deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability
-
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
additional information
-
a truncated protein (having 1-167 amino acids, molecular weight ,18 kDa) is generated: The truncated protein shows a 3.5fold reduction in the oxidation rate of Fe(II). Lack of C-terminus has an impact of the stability of the protein. Truncated BfrB starts unfolding on exposure to even a very low temperature of 30°C whereas the native protein remains almost unaffected till 50°C before denaturing rapidly
additional information
-
truncation of the C-terminal transmembrane domain leading to a soluble enzyme form, sFet3p, that is secreted from the cell, structure comparison with the wild-type enzyme, overview. The apparent trafficking defect observed with alanine substitution at some asparagines in sFet3p is not observed in the full-length, membrane-tethered protein
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Homo sapiens
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A kinetic study on the phenothiazine dependent oxidation of NADH by bovine ceruloplasmin
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-
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Homo sapiens
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Homo sapiens
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Escherichia coli (P0ABD3), Escherichia coli
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Mus musculus
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