Information on EC 1.16.3.1 - ferroxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.16.3.1
-
RECOMMENDED NAME
GeneOntology No.
ferroxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
non-pathway related
-
-
Porphyrin and chlorophyll metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mushroom
-
-
Manually annotated by BRENDA team
goose
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
turtle
-
-
Manually annotated by BRENDA team
strain 17D-
-
-
Manually annotated by BRENDA team
no activity in Rana catesbeiana
bullfrog
-
-
Manually annotated by BRENDA team
sheep
-
-
Manually annotated by BRENDA team
frog
-
-
Manually annotated by BRENDA team
two Dps proteins, DpsA-Te and Dps-Te, encoded by the two genes tll2470 and tll0614 or dpsA-Te and dps-Te, respectively
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + Cu2+ + O2
?
show the reaction diagram
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulphonic acid + Cu(I) + O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + Cu(I) + O2
?
show the reaction diagram
-
-
-
-
?
2-chloro-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-methoxy-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-methyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-nitro-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
2-sulfonic acid-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
4 Cu+ + 4 H+ + O2
4 Cu2+ + 2 H2O
show the reaction diagram
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
4 Mn(II) + 4 H+ + O2
4 Mn(III) + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Mn(III) + 4 H+ + O2
4 Mn(IV) + 2 H2O
show the reaction diagram
-
-
-
-
?
4-methylcatechol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
4-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxyindol-3-ylacetic acid + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptophan + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
5-hydroxytryptophol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
alimemazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
show the reaction diagram
apotransferrin + Fe2+ + O2
diferric transferrin + H2O
show the reaction diagram
-
-
-
-
?
ascorbate + Fe2+ + O2
?
show the reaction diagram
catechol + Fe2+ + O2
?
show the reaction diagram
catechol + O2
?
show the reaction diagram
-
mushroom tyrosinase is able to catalyse the oxidation of Fe2+ to Fe3+
-
-
?
chlorpromazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
Cu+ + H+ + O2
Cu2+ + H2O
show the reaction diagram
diethazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
dihydroxyphenylethylamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
durenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
show the reaction diagram
-
-
-
-
?
Fe(II) + hydroquinone + O2
Fe(III) + ? + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
ferrous ammonium sulfate + O2
?
show the reaction diagram
-
-
-
-
?
ferrous ammonium sulfate + O2
? + H2O
show the reaction diagram
-
-
-
-
?
fluphenazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
hydroquinone + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
show the reaction diagram
L-norepinephrine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
m-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
monophenol + O2
catechol + H2O
show the reaction diagram
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Cu2+ + O2
N,N'-dimethyl-p-phenylenediamine radical + Cu+
show the reaction diagram
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
N,N'-dimethyl-p-phenylenediamine + Fe3+ + O2
?
show the reaction diagram
-
-
-
-
?
N,N,N',N'-tetramethyl-p-phenylenediamine + Fe2+
?
show the reaction diagram
-
-
-
-
?
N,N-diethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-m-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N-(p-methoxyphenyl)-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N-acetyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N-ethyl-N-(2-hydroxyethyl)-p-phenylenediamine Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
N-phenyl-p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
NADH + O2
NAD+ + H2O
show the reaction diagram
-
-
-
-
?
o-aminophenol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
show the reaction diagram
o-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
p-aminophenol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-anisidine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Cu2+ + O2
p-phenylenediamine radical + Cu+
show the reaction diagram
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
periciazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
perphenazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
prochlorperazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
promazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
prometazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
pyrogallol + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
quinone + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
thioridazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
trifluoperazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
triflupromazine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
inhibits enzymatic activity
copper
Cr3+
-
0.1 M, activity 102%
Cu
-
4 atoms per protein
Fe(II)
Ni2+
-
activating
phosphate
-
phosphate does not affect the oxidation rate of the first 48 Fe(II) per ferritin aerobically added to apoferritin. But, it does increase the iron-oxidation rate of subsequent additions of 48 Fe(II) per ferritin by a factor of 6. Phosphate increases the oxidation rate of iron
vanadate
-
increases the oxidation rate of iron
additional information
-
also other oxoanions, besides phosphate and vanadate, increase the oxidation rate of iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-Aminohexanoic acid
-
-
Ba2+
-
weak inhibitor
Bathocuproine disulfonate
-
incubation of C6 glioma cells with the copper chelator bathocuproine disulfonate prevents expression of ceruloplasmin on the cell surface and leads to a decrease in cellular ceruloplasmin. Incubation of cells with bathocuproine disulfonate also reduces the ability of cells to lower their ferritin levels
bathocuproinedisulfonic acid
-
-
Ca2+
-
weak inhibitor
catalase
-
catalase in the assay system results in little inhibition of the ferroxidase activity of xanthine oxidoreductase
-
Cr3+
-
strong inhibitor
fluoride
-
treatment of rabbits with standard common rabbit diet and water ad libitum containing 40 mg fluoride per liter results in significant decrease of ceruloplasmin level in serum by days 35 and 70, with concomitant increase of serum adenosine eaminase and C-reactive protein
K+
-
weak inhibitor
Li+
-
weak inhibitor
N3-
-
anion behaves as an inhibitor of the oxidase activity versus Fe2+
Na+
-
weak inhibitor
SDS
-
enzymatic activity inhibited with 1% SDS
Sn2+
-
weak inhibitor
Sodium azide
Superoxide dismutase
-
superoxide dismutase in the assay system results in little inhibition of the ferroxidase activity of xanthine oxidoreductase
-
terbium
above 0.2 mM, complete abolition of iron binding. Crystal structure of enzyme complex at 2.1 A resolution, terbium binds to the ferroxidase center
additional information
-
core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chlorpromazine
-
formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule
CuCl2
-
increase in enzyme mRNA due to transcriptional activation of enzyme genes promoter
Iron
-
an iron deficient diet fed over 12 months increases expression of enterocyte hephaestin; an iron overload diet fed over 6 months increases expression of ferritin in liver and enterocytes
lactoferrin
-
apolactoferrin increases the oxidation rate of Fe(II) by ceruloplasmin 1.25fold at pH 5.5. Lactoferrin saturated with Fe3+ or Cu2+ increases the oxidation rate of Fe2+ 1.6fold when in 1:1 ratio with enzyme
-
levopromazine
-
formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule
promazine
-
formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule
pyrrolidine dithiocarbamate
-
regulation of ceruloplasmin expression by a copper-dependent transcriptional mechanism
triflupromazine
-
formation of a complex with ceroluplasmin and stimulation. Good correlation of stability of enzyme-drug complex and electron donor ability of the drug molecule
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.241
2-chloro-p-phenylenediamine
-
-
0.161
2-methoxy-p-phenylenediamine
-
-
0.213
2-methyl-p-phenylenediamine
-
-
0.00126
2-nitro-p-phenylenediamine
-
-
0.00262
2-sulfonic acid-p-phenylenediamine
-
-
0.00285
3,4-Dihydroxyphenethylamine
-
-
0.0603
4-Methylcatechol
-
-
0.0015
4-phenylenediamine
-
pH 5, 20C
0.00834
5-hydroxyindol-3-ylacetic acid
-
-
0.908
5-hydroxytryptamine
-
-
0.0163
5-hydroxytryptophan
-
-
0.0051
5-hydroxytryptophol
-
-
0.0014
alimemazine
-
-
0.0052
ascorbate
-
-
0.282
catechol
-
-
0.0035
chlorpromazine
-
-
0.00002 - 0.081
Cu+
0.0023
diethazine
-
-
0.171
durenediamine
-
-
0.0049 - 3.994
Fe(II)
0.0006 - 14.1
Fe2+
0.0021
Ferrous ammonium sulfate
-
pH 5.0, 22C
0.005
fluphenazine
-
-
0.018 - 30.5
hydroquinone
0.00255 - 5.8
L-epinephrine
0.00281
L-norepinephrine
-
-
0.036
m-phenylenediamine
-
-
0.06 - 0.164
N,N'-dimethyl-p-phenylenediamine
0.197
N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
0.556
N,N-diethyl-p-phenylenediamine
-
-
0.00305
N,N-dimethyl-m-phenylenediamine
-
-
0.203
N,N-Dimethyl-p-phenylenediamine
-
-
0.021
N-(p-methoxyphenyl)p-phenylenediamine
-
-
0.0123
N-acetyl-p-phenylenediamine
-
-
0.11
N-ethyl-N-(2-hydroxyethyl)p-phenylenediamine
-
-
0.087
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine
-
-
0.048
N-phenyl-p-phenylenediamine
-
-
0.14 - 0.23
NADH
0.00288
o-aminophenol
-
-
0.12 - 0.76
o-Dianisidine
0.00295 - 4.15
o-phenylenediamine
0.0011 - 0.0632
O2
0.00154
p-Aminophenol
-
-
0.00614
p-anisidine
-
-
0.005 - 2.5
p-phenylenediamine
0.002
periciazine
-
-
0.0013
perphenazine
-
-
0.9
prochlorperazine
-
-
0.0013
promazine
-
-
0.0023
Promethazine
-
-
0.0579
pyrogallol
-
-
0.0657
quinone
-
-
0.0014
thioridazine
-
-
0.0028
Trifluoperazine
-
-
0.01
triflupromazine
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.15
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulphonic acid
Rhodococcus erythropolis
-
pH 5.5, 30C
0.48
4-phenylenediamine
Homo sapiens
-
pH 5, 20C
0.038 - 15.8
Cu+
0.232 - 6.08
Fe(II)
0.07 - 3.91
Fe2+
0.39 - 7.2
hydroquinone
0.37 - 4.8
p-phenylenediamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000039 - 0.00008
Cu+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.25
in an Erel assay measuring loss of Fe2+
0.28
-
-
0.29
-
p-phenylenediamine as substrate
0.3
in a transferrin assay measuring transformation of apotransferrin to holotransferrin
0.58
-
in an Erel assay measuring loss of Fe2+
0.88
-
o-dianisidine as substrate
1.15
-
o-dianisidine as substrate
1.73
-
p-phenylenediamine as substrate
3.13
-
-
3.29
-
o-dianisidine as substrate
5.72
-
p-phenylenediamine as substrate
30
-
ferroxidase II
additional information
-
MCO1 has ferroxidase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.2
-
schizophrenics
5.5 - 5.6
-
normal persons
5.7
-
phosphate buffer
5.8
-
p-phenylenediamine as substrate
6.8
-
-
7.4
-
xanthine oxidoreductase with ferroxidase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
-
-
6 - 8
-
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 25
-
assay at
23
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of cortex
Manually annotated by BRENDA team
-
in fluid from patients with Parkinson's disease, Alzheimer's disease, Huntington's disease, a significantly decreased ferroxidase activity is found agreeing with findings of iron deposition in these entities, while free copper is found to be increased in cerebrospinal fluid and appears to be a good biomarker of Parkinson's disease. The sum of nitrites and nitrates as end products of nitric oxide are increased in the degenerative diseases Parkinson's disease, Alzheimer's disease, Huntington's disease and lateral amyotrophic sclerosis and fluorescent lipoperoxidation products in three of them, excepting lateral amyotrophic sclerosis
Manually annotated by BRENDA team
-
epithelial cells
Manually annotated by BRENDA team
-
vascular epithelial cell
Manually annotated by BRENDA team
-
nonadherent cells, T and B lymphocytes
Manually annotated by BRENDA team
-
basal surface of midgut
Manually annotated by BRENDA team
-
mouse embryonal carcinoma cell line, addition of enzyme to culture medium induces aggregation within 24 h, with half-maximal effect at 0.05 mM. No association with apoptosis, necrosis or changes in secretory function. aggregation is less pronounce in aging neurons, K+ channels seem not to be involved
Manually annotated by BRENDA team
-
nephrotic urine
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
possible localization of the protein at the thylakoid membranes due to presence of a long hydrophobic N-terminal tail
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Lithobates catesbeiana
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)