1.16.3.1: ferroxidase
This is an abbreviated version!
For detailed information about ferroxidase, go to the full flat file.
Word Map on EC 1.16.3.1
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1.16.3.1
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transferrin
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hemoglobin
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anemia
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women
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overload
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children
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c-reactive
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albumin
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erythrocyte
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marrow
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hematological
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pregnancy
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hepcidin
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erythropoietin
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hematocrit
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dialysis
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hereditary
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infant
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spleen
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hemodialysis
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ferric
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thalassemia
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covid-19
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iron-deficient
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ferrous
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fever
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haptoglobin
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corpuscular
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reticulocyte
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admitted
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iron-binding
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micronutrient
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folate
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admission
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wilson
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creatinine
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fibrinogen
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transfusions
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demographic
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beta-thalassemia
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bilirubin
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sickle
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transfused
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acute-phase
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coronavirus
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protoporphyrin
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anthropometric
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d-dimer
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deferoxamine
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biotechnology
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analysis
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hemoglobinopathy
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nutrition
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medicine
- 1.16.3.1
- transferrin
- hemoglobin
- anemia
- women
- overload
- children
-
c-reactive
- albumin
- erythrocyte
- marrow
- hematological
- pregnancy
- hepcidin
- erythropoietin
-
hematocrit
- dialysis
- hereditary
- infant
- spleen
-
hemodialysis
-
ferric
- thalassemia
- covid-19
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iron-deficient
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ferrous
- fever
- haptoglobin
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corpuscular
- reticulocyte
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admitted
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iron-binding
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micronutrient
- folate
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admission
- wilson
- creatinine
- fibrinogen
- transfusions
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demographic
- beta-thalassemia
- bilirubin
-
sickle
-
transfused
-
acute-phase
- coronavirus
- protoporphyrin
-
anthropometric
-
d-dimer
- deferoxamine
- biotechnology
- analysis
- hemoglobinopathy
- nutrition
- medicine
Reaction
4 Fe(II)
+
4 H+
+
Synonyms
AfFtn, apoferritin, bacterial ferritin, bacterial ferroxidase, bacterioferritin, bacterioferritin B, BFR, BfrB, blue copper oxidase, caeruloplasmin, ceruloplasmin, Cp115, Cp135, Cp200, CT1740, CtFtn, cyto-FOX, cytosolic FOX, DdBfr, Dpr, Dps, Dps protein, Dps-like peroxide resistance protein, Dps-Te, DpsA, DpsA-Te, DspA, EncA, encapsulin, encapsulin A, ferritin, ferro-O2-oxidoreductase, ferro:O2 oxidoreductase, ferroxidase, ferroxidase center of bacterioferritin, ferroxidase I, ferroxidase II, ferroxidase, iron II:oxygen oxidoreductase, Fet3, FET3 gene product, fet3p, FOX1, Ftn, FtnA, H ferritin, H' ferritin, H-chain ferritin, Helicobacter pylori neutrophil-activating protein, hephaestin, HP-NAP, HuHF, human ceruloplasmin form I, human H ferritin, human H-chain ferritin, iron(II): oxygen oxidoreductase, L-ferritin, M ferritin, MaDps, MCO1, MmcO, mnxDEFG, monophenol-o-monoxygenase, More, mouse ceruloplasmin, multicopper ferroxidase, multicopper oxidase, multicopper oxidase 1, multicopper oxidase CueO, multicopper oxidase-1, mushroom tyrosinase, mycobacterial multicopper oxidase, neutrophil-activating protein, non-ceruloplasmin ferroxidase, non-specific DNA-binding protein Dps/ferroxidase, rhHp, rHuHF, Rv0846c, serum ferroxidase, VcDps, VCE_000308, xanthine oxidoreductase
ECTree
1.16.3.1 ferroxidaseAdvanced search results
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results (Engineering
Engineering on EC 1.16.3.1 - ferroxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E184A
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a Fet34 mutant, that shows altered kinetics compared to the wild-type enzyme
E184A/D408A
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a Fet34 mutant, that shows altered kinetics compared to the wild-type enzyme
A19Y
R454A
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Arg454 is mutated to Ala in order to reduce proteolytic cleavage
M358S/M361S/M362S/M364S/M366S
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
M358S/M361S/M362S/M364S/M366S
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mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
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D616A/H621A/E960A/H965A
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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
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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
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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
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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/E27D
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in X-ray absorption same properties as wild-type, but reduced reduction activity
H31G
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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
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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
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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
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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
E136A
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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
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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
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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
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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
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putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity
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C486A
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cysteine 486 is required for MmcO activity. Mutation results in inactive Rv0846c protein which does not protect Mycobacterium tuberculosis against copper stress
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D278A
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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
D283A
D409A
E185A
E185A/D409A
E185A/Y354A
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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
E185D
N113A
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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
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site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics
N198A
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site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics
N244A
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site-directed mutagenesis of a potential N-glycosylation site
N265A
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site-directed mutagenesis of a potential N-glycosylation site
N27A
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site-directed mutagenesis of a potential N-glycosylation site
N292A
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site-directed mutagenesis of a potential N-glycosylation site
N300A
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site-directed mutagenesis of a potential N-glycosylation site
N359A
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site-directed mutagenesis of a potential N-glycosylation site
N381A
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site-directed mutagenesis of a potential N-glycosylation site
N74A
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site-directed mutagenesis of a potential N-glycosylation site
N77A
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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
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site-directed mutagenesis of a potential N-glycosylation site
T307A
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site-directed mutagenesis of a potential O-glycosylation site
Y354A
Y354F
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
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interactions of mutant D74A with various divalent ions compared to the wild-type enzyme, overview
additional information
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
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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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
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D283A
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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
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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
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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
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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
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increase in reduction potential by 120 mV, complete loss of specificity for Fe(II), functions kinetically as an inefficient laccase
E185A/D409A
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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
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2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type
E185D
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normal absorbance at 330 nm and 608 nm due to type 3 and type 1 copper sites, EPR spectra equivalent to wild-type
Y354A
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2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type
Y354A
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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
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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
Acidomyces acidophilus 26774
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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
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additional information
deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability
additional information
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deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability
additional information
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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deletion of 38 amino acid of the C-terminal region of rCtFtn decreases the enzyme stability
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additional information
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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
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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
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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
