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
1.16.3.1
-
RECOMMENDED NAME
GeneOntology No.
ferroxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
show the reaction diagram
A multi-copper protein: ceruloplasmin from animals, rusticyanin in Thiobacillus ferroxidans
-
-
-
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
show the reaction diagram
iron binding site plays a major role in tuning the reduction potenzial of iron to provide a large driving force for the reaction, E185 residue provides the dominant electron transfer pathway to the T1 Cu site
-
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
show the reaction diagram
steady state kinetic analysis, 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
show the reaction diagram
residues D283, E185, D409 provide a Fe(II) binding site that favors ferric ion thus reducing the reduction potential of the bound Fe(II). Residues E185 and D409 form part of the electron-transfer pathway from the bound Fe(II) to the proteins type I Cu(II)
-
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
show the reaction diagram
reaction mechanism, overview. Two reaction steps: 1. 2 Fe2+ O2 + 2 H+ = 2 Fe3+ + H2O2 and 2. H2O2 + 2 Fe2+ + 2 H+ = 2 Fe3+ + 2 H2O. The second step is rate-limiting
Q8DL82
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
conversions
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
apoferritin
-
-
bacterioferritin
-
-
bacterioferritin B
-
-
BFR
P0ABD3
-
blue copper oxidase
-
-
caeruloplasmin
-
-
-
-
ceruloplasmin
-
-
-
-
Cp115
-
-
Cp135
-
-
Cp200
-
-
cyto-FOX
-
-
cytosolic FOX
-
-
DdBfr
-
Desulfovibrio desulfuricans bacterioferritin
Dpr
Q99YU7
DNA-binding protein from starved cells
Dps
Q7CN02
i.e. DNA-binding proteins from starved cells
Dps protein
P80725
-
Dps-like peroxide resistance protein
Q7CN02
-
Dps-like peroxide resistance protein
-
-
ferritin
-
-
ferritin
P07798
-
ferro-O2-oxidoreductase
-
-
ferro:O2 oxidoreductase
-
-
-
-
ferroxidase
A8IZT9
-
ferroxidase
Chlamydomonas reinhardtii 17D-
-
-
-
ferroxidase
Rattus norvegicus Sprague-Dawley
-
-
-
ferroxidase center of bacterioferritin
P0ABD3
-
ferroxidase I
-
-
-
-
ferroxidase II
-
-
ferroxidase, iron II:oxygen oxidoreductase
-
-
-
-
FET3 gene product
-
-
FOX1
Chlamydomonas reinhardtii 17D-
-
-
-
H ferritin
P02794
-
H-chain ferritin
-
-
hephaestin
-
-
hephaestin
-
-
HP-NAP
G1UIZ2
-
HuHF
-
-
HuHF
P02794
-
human ceruloplasmin form I
-
-
human H ferritin
P02794
-
human H-chain ferritin
-
-
iron(II): oxygen oxidoreductase
-
-
-
-
mnxDEFG
-
-
mouse ceruloplasmin
-
ceruloplasmin with ferroxidase activity detected by native PAGE
multicopper ferroxidase
-
-
multicopper oxidase
-
-
multicopper oxidase
-
-
multicopper oxidase
-
-
multicopper oxidase
-
-
multicopper oxidase-1
-
-
mushroom tyrosinase
-
-
mycobacterial multicopper oxidase
I6WZK7
-
mycobacterial multicopper oxidase
I6WZK7
-
-
neutrophil-activating protein
G1UIZ2
-
non-ceruloplasmin ferroxidase
-
-
rhHp
-
-
rHuHF
-
recombinant human H-chain ferritin
Rv0846c
I6WZK7
locus
Rv0846c
I6WZK7
locus
-
serum ferroxidase
-
-
xanthine oxidoreductase
-
-
monophenol-o-monoxygenase
-
-
additional information
-
enzyme possesses EC 1.10.3.2 laccase activity
CAS REGISTRY NUMBER
COMMENTARY
9031-37-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mushroom
-
-
Manually annotated by BRENDA team
goose
-
-
Manually annotated by BRENDA team
cow
-
-
Manually annotated by BRENDA team
turtle
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 17D-
strain 17D-
-
-
Manually annotated by BRENDA team
strain JM109 and strain BL21(DE3)pLysS
UniProt
Manually annotated by BRENDA team
children with Henoch-Schoenlein purpura
-
-
Manually annotated by BRENDA team
Cohn's fraction F-IV-1 of normal human pooled plasma; human
-
-
Manually annotated by BRENDA team
commercial product ceruloplasmin
-
-
Manually annotated by BRENDA team
ferritin heavy chain
UniProt
Manually annotated by BRENDA team
human; human hepatoblastoma cell line HepG2
-
-
Manually annotated by BRENDA team
multicopper oxidase hephaestin, with additional ferroxidase activity. Expression in baby hamster kidney cells
-
-
Manually annotated by BRENDA team
patients with chronic lymphocytic leukemia
-
-
Manually annotated by BRENDA team
patients with Parkinson's disease, Alzheimer's disease, Huntington's disease and lateral amyotrophic sclerosis
-
-
Manually annotated by BRENDA team
patients with Wilson disease and ATP7B genotypes
-
-
Manually annotated by BRENDA team
hypoxic mice
-
-
Manually annotated by BRENDA team
wild-type and ceruloplasmin knockout mice
Uniprot
Manually annotated by BRENDA team
wild-type and ceruloplasmin knockout mice based on strain C57BL/6 J
-
-
Manually annotated by BRENDA team
no activity in Rana catesbeiana
bullfrog
-
-
Manually annotated by BRENDA team
frog
-
-
Manually annotated by BRENDA team
rat; Sprague-Dawley
-
-
Manually annotated by BRENDA team
strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
hog; pig, porcine
-
-
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
LITERATURE
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
I6WZK7
the susceptibility of the DELTAmmcO mutant to copper in vitro is increased more than 10fold compared to that of wild-type Mycobacterium tuberculosis, indicating that MmcO also oxidizes toxic Cu(I)
physiological function
Q99YU7
binding and oxidization of iron, thus preventing the formation of harmful reactive oxygen species
physiological function
A8IZT9
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
Q7CN02
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
Q8DL82
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
I6WZK7
MmcO is required for copper resistance in Mycobacterium tuberculosis
physiological function
-
MmcO is required for copper resistance in Mycobacterium tuberculosis
-
physiological function
Chlamydomonas reinhardtii 17D-
-
FOX1 is important for iron uptake in a situation of iron deficiency
-
malfunction
-
the susceptibility of the DELTAmmcO mutant to copper in vitro is increased more than 10fold compared to that of wild-type Mycobacterium tuberculosis, indicating that MmcO also oxidizes toxic Cu(I)
-
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
Q8DL82
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
P02794
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + Cu2+ + O2
?
show the reaction diagram
I6WZK7
-
-
-
?
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 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
Q8DL82
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
I6WZK7
MmcO also has ferroxidase activity
-
-
?
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
Q61147
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
show the reaction diagram
Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
-
-
-
-
?
apotransferrin + Fe2+ + O2
diferric transferrin + H2O
show the reaction diagram
-
-
-
-
?
ascorbate + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
ascorbate + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
catechol + 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
-
-
-
-
?
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
Q61147
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
P00450
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
iron acquisition pathway
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
multicopper oxidase essential for normal iron homeostasis
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
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-epinephrine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
L-norepinephrine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
m-phenylenediamine + Fe2+ + O2
?
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 + 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-dianisidine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
-
o-dianisidine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
o-phenylenediamine + 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
-
oxidation through this iron-ferroxidase-coupled system is faster than direct oxidation by the enzyme, without iron p-phenylenediamine is directly oxidized by the enzyme-bound copper
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
show the reaction diagram
-
no p-phenylenediamine oxidase activity by ferroxidase II
-
-
-
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
-
-
-
-
?
monophenol + O2
catechol + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
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
?
-
-
ascorbate and aromatic amines are not directly oxidized by the enzyme, but through an iron-ferroxidase-coupled system in which iron is an electron mediator between the substance and the enzyme
-
-
-
additional information
?
-
-
caeruloplasmin inhibits lipid peroxidation and deoxyribose degradation stimulated by iron and copper salts
-
-
-
additional information
?
-
-
only ceruloplasmin capable of complete reoxidation by oxygen
-
-
-
additional information
?
-
-
ferroxidase II does not catalyze the oxidation of benzylamine
-
-
-
additional information
?
-
-
ascorbate oxidase EC 1.10.3.3 activity
-
-
-
additional information
?
-
-
possesses superoxide dismutase activity
-
-
-
additional information
?
-
-
Fet3p is able to catalyze effectively the incorporation of iron onto apotransferrin
-
-
-
additional information
?
-
-
ferroxidase oxidizes in the presence of trace amounts of iron certain substances auch as ascorbate, catechol and hydroquinone, which are not true substrates but can react with Fe3+ in a cyclic reaction
-
-
-
additional information
?
-
-
developmental role of enzyme in nervous system organization
-
-
-
additional information
?
-
-
enzyme is involved in conferring peroxide tolerance to the bacterium
-
-
-
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
?
-
Q7CN02
Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface
-
-
-
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
?
-
-
the non-heme iron-containing ferritin has dual ferroxidase and DNA-binding activities, overview
-
-
-
additional information
?
-
-
competitive binding with Zn2+
-
-
-
additional information
?
-
Q7CN02
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
?
-
-
enzymatic activity of sFet34 towards ferrous iron is determined by quantifying the velocity of O2 uptake using standard O2-electrode protocols
-
-
-
additional information
?
-
P02794
enzyme metal binding structure, 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
?
-
-
Mn oxidation from soluble Mn(II) to Mn(IV) oxides is a two-step reaction catalyzed by an MCO-containing complex
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
Q8DL82
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
P00450
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
iron acquisition pathway
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
-
multicopper oxidase essential for normal iron homeostasis
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
additional information
?
-
-
developmental role of enzyme in nervous system organization
-
-
-
additional information
?
-
-
enzyme is involved in conferring peroxide tolerance to the bacterium
-
-
-
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
?
-
Q7CN02
Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface
-
-
-
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
?
-
-
the non-heme iron-containing ferritin has dual ferroxidase and DNA-binding activities, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
-
inhibits enzymatic activity
Cd2+
-
-
Cd2+
-
activating
Cd2+
G1UIZ2
crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC)
Co2+
-
-
Co2+
-
activating
copper
-
3.1 atoms per protein molecule
copper
A8IZT9
an InterPro Scan domain search predicted that Fox1 contains six cupredoxin domains
copper
I6WZK7
increases activity
Cr3+
-
0.1 M, activity 102%
Cu
-
4 atoms per protein
Cu2+
-
copper-binding protein
Cu2+
-
-
Cu2+
-
Fet31 and Fet34 contain a type 3 Cu2+ pair known as the binuclear Cu-cluster, recombinant soluble Fet34 contains a full complement of 4 Cu atoms per molecule
Cu2+
-
upon incubation with Cu2+ ions, low active apo-CueOR is converted into the active holo-CueOR in vivo
Fe(II)
-
wild-type, Km value 0.005 mM, mutant D283A, 0.019 mM, mutant E185A, 0.036 mM, mutant D409A, 0.019 mm, mutant E185A/D409A, 4 mM, respectively. The protein provides a binding site for Fe(II) that actually favors Fe(III), this coordination sphere places the bound Fe(II) in a state of entasis that can be relieved by loss of an electron. The EO of the bound Fe(II) is lowered relative to that of aqueous ferrous iron making electron transfer thermodynamically favorable. Carboxylates within this coordination sphere provide an electronic coupling pathway for the electron transfer via their H-bond network with type 1 Cu-histidine ligands thus making electron transfer kinetically efficient
Fe(II)
-
the active site within each subunit consists of two inequivalent fivecoordinate ferrous centers that are weakly antiferromagnetically coupled, consistent with a my-1,3 carboxylate bridge. The active site ligand set is unusual and likely includes a terminal water bound to each Fe(II) center. The Fe(II) ions bind to the active sites in a concerted manner, and cooperativity among the sites in each subunit is observed
Fe2+
-
potent activator in the oxidation of many aromatic amines and ascorbate catalyzed by ferroxidase
Fe2+
-
substrate and activator for ferroxidase
Fe2+
-
rhHp possesses both high-affinity and low-affinity binding sites for ferrous iron
Iron
-
ceruloplasmin is regulated by cellular iron status
Iron
-
12 molecules per dodecamer
Iron
-
decrease of ceruloplasmin expression in cerebral ischemia correlates negatively with iron concentration
Iron
P80725
-
Mg2+
-
-
Mg2+
-
activating
Mn2+
-
-
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
Zn2+
-
activating
Zn2+
Q8DL82
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
Zn2+
G1UIZ2
crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC)
Mn2+
-
activating
additional information
-
also other oxoanions, besides phosphate and vanadate, increase the oxidation rate of iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-Aminohexanoic acid
-
-
Al3+
-
-
Al3+
-
strong inhibitor
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
-
Ce3+
-
-
Ce3+
-
strong inhibitor
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
Ga3+
-
-
Ga3+
-
strong inhibitor
In3+
-
-
-
In3+
-
strong inhibitor
-
K+
-
weak inhibitor
La3+
-
-
La3+
-
strong inhibitor
N3-
-
anion behaves as an inhibitor of the oxidase activity versus Fe2+
Na+
-
weak inhibitor
Rh3+
-
-
Rh3+
-
strong inhibitor
Sc3+
-
-
Sc3+
-
strong inhibitor
SDS
-
enzymatic activity inhibited with 1% SDS
Sn2+
-
weak inhibitor
Sodium azide
-
no inhibition of ferroxidase II
Sodium azide
-
amine oxidase activity is sensitive to inhibition by sodium azide
Sodium azide
-
-
Sodium azide
-
irreversible inhibitor
Sodium azide
-
1-2.5 mM sodium azide reduces ferroxidase activity markedly
Sodium azide
Q61147
1-2.5 mM sodium azide reduces ferroxidase activity markedly
Sodium azide
-
1-2.5 mM sodium azide reduces ferroxidase activity markedly
Superoxide dismutase
-
superoxide dismutase in the assay system results in little inhibition of the ferroxidase activity of xanthine oxidoreductase
-
terbium
P80725
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
VO2+
-
-
VO2+
-
strong inhibitor
Y3+
-
strong inhibitor
Zinc
P80725
above 0.2 mM, complete abolition of iron binding. Crystal structure of enzyme complex at 1.8 A resolution, zinc binds to the ferroxidase center. Residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, and Streptococcus sanguinis Dpr proteins
Zinc
-
residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, Listeria innocua, and Streptococcus sanguinis Dpr proteins
Zn2+
-
-
Zn2+
P0ABD3
50 Zn2+ ions per bacterioferritin blocked binding of Fe2+
Zn2+
-
2 M Zn2+ occupies the ferroxidase center as redox-invariant analogue of Fe2+
ZrO2+
-
-
ZrO2+
-
strong inhibitor
Li+
-
weak inhibitor
additional information
-
core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
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
Cu+
-
pH 5.5, 30C, mutant containing a deleted methionine-rich C-terminal tail
0.00008
Cu+
-
pH 5.5, 30C, wild-type
0.0368
Cu+
-
pH 5.0
0.0379
Cu+
-
pH 5.0
0.081
Cu+
-
Cu+ oxidation, pH 5, 23C, wild-type
0.0023
diethazine
-
-
0.171
durenediamine
-
-
0.0049
Fe(II)
-
wild-type, pH 6.0
0.0188
Fe(II)
-
mutant D409A, pH 6.0
0.0193
Fe(II)
-
mutant D283A, pH 6.0
0.0356
Fe(II)
-
mutant E185A, pH 6.0
3.994
Fe(II)
-
mutant E185A/D409A, pH 6.0
0.0006
Fe2+
-
pH 6.5, 30C, 2 Km-values: 0.0006 and 0.050 mM
0.0035
Fe2+
-
pH 5, 20C, Km for high-affinity iron-binding sites using a two-component Eadie-Hofstee plot, Vmax: 67 nmol/min
0.0039
Fe2+
-
-
0.004
Fe2+
-
pH 5, 20C
0.0048
Fe2+
-
wild-type, pH 6.0
0.0054
Fe2+
-
pH 5.0
0.0058
Fe2+
-
mutant Y354F, pH 6.0
0.0079
Fe2+
-
recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication
0.0083
Fe2+
-
pH 5.0
0.0086
Fe2+
-
mutant E185D, pH 6.0
0.0107
Fe2+
-
pH 5, 20C, Km for low-affinity iron-binding sites using a two-component Eadie-Hofstee plot, Vmax: 286 nmol/min
0.0108
Fe2+
-
recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication
0.011
Fe2+
-
mutant D278A, pH 6.0
0.017
Fe2+
-
mutant Y354A, pH 6.0
0.04
Fe2+
-
mutant E185A, pH 6.0
0.046
Fe2+
-
xanthine oxidoreductase with ferroxidase activity
0.05
Fe2+
-
pH 6.5, 30C, 2 Km-values: 0.0006 and 0.050 mM
0.1 - 2
Fe2+
-
Fe2+ oxidation, pH 5, 23C, wild-type
0.12
Fe2+
-
-
0.125
Fe2+
-
-
0.13
Fe2+
-
-
0.135
Fe2+
-
Fe2+ oxidation, pH 5, 23C, mutant M358S/M361S/M362S/M364S/M366S/M368S
0.15
Fe2+
-
-
1.43
Fe2+
-
recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication
3
Fe2+
-
wild-type, pH 6.5, 4C
3.51
Fe2+
-
mutant E185A/Y354A, pH 6.0
4.6
Fe2+
-
mutant Y354A, pH 6.5, 4C
8.2
Fe2+
-
mutant E185D, pH 6.5, 4C
12.7
Fe2+
-
mutant Y354F, pH 6.5, 4C
14.1
Fe2+
-
mutant E185A, pH 6.5, 4C
0.0021
Ferrous ammonium sulfate
-
pH 5.0, 22C
0.005
fluphenazine
-
-
0.018
hydroquinone
-
mutant E185A
0.019
hydroquinone
-
mutant D283A
0.025
hydroquinone
-
wild-type
0.03
hydroquinone
-
mutant D409A; mutant E185A/D409A
3
hydroquinone
-
wild-type, pH 6.5, 25C
3
hydroquinone
-
wild-type, pH 6.0
4.3
hydroquinone
-
mutant D278A, pH 6.0
4.6
hydroquinone
-
mutant Y354A, pH 6.5, 25C
4.6
hydroquinone
-
mutant Y354A, pH 6.0
8.2
hydroquinone
-
mutant E185D, pH 6.5, 25C
8.2
hydroquinone
-
mutant E185D, pH 6.0
12.7
hydroquinone
-
mutant Y354F, pH 6.5, 25C
12.7
hydroquinone
-
mutant Y354F, pH 6.0
14.1
hydroquinone
-
mutant E185A, pH 6.5, 25C
14.1
hydroquinone
-
mutant E185A, pH 6.0
16.9
hydroquinone
-
mutant E185A/Y354A, pH 6.0
18.2
hydroquinone
-
mutant E185A, pH 6.0
19.3
hydroquinone
-
mutant D283A, pH 6.0
25.5
hydroquinone
-
wild-type, pH 6.0
30.3
hydroquinone
-
mutant D409A, pH 6.0
30.5
hydroquinone
-
mutant E185A/D409A, pH 6.0
0.00255
L-epinephrine
-
-
5.8
L-epinephrine
-
-
0.00281
L-norepinephrine
-
-
0.06
N,N'-dimethyl-p-phenylenediamine
-
-
0.11
N,N'-dimethyl-p-phenylenediamine
-
-
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
NADH
-
pH 6.0, 30C, presence of triflupromazine
0.21
NADH
-
pH 6.0, 30C, presence of levomepromazine
0.22
NADH
-
pH 6.0, 30C, presence of chlorpromazine
0.23
NADH
-
pH 6.0, 30C, presence of promazine
0.00288
o-aminophenol
-
-
0.12
o-Dianisidine
-
-
0.15
o-Dianisidine
-
-
0.18
o-Dianisidine
-
-
0.43
o-Dianisidine
-
-
0.76
o-Dianisidine
-
-
0.00295
o-phenylenediamine
-
-
4.15
o-phenylenediamine
-
-
0.0074
O2
-
pH 7.0, 0.2 M phosphate buffer
0.009
O2
-
-
0.0182
O2
-
pH 7.0, 0.2 M acetate buffer
0.0276
O2
-
pH 5.2, 0.0133 M phosphate buffer
0.0286
O2
-
pH 5.4, 0.2 M acetate buffer
0.05
O2
-
xanthine oxidoreductase with ferroxidase activity
0.0554
O2
-
pH 6.3, 0.0133 M phosphate buffer
0.0632
O2
-
pH 6.5, 0.2 M acetate buffer
0.00154
p-Aminophenol
-
-
0.00614
p-anisidine
-
-
0.005
p-phenylenediamine
-
mutant D278A, pH 6.0
0.008
p-phenylenediamine
-
mutant Y354A, pH 6.0
0.0084
p-phenylenediamine
-
wild-type, pH 6.0
0.0143
p-phenylenediamine
-
mutant Y354F, pH 6.0
0.019
p-phenylenediamine
-
-
0.0228
p-phenylenediamine
-
mutant E185D, pH 6.0
0.0333
p-phenylenediamine
-
mutant E185A, pH 6.0
0.053
p-phenylenediamine
-
-
0.0705
p-phenylenediamine
-
mutant E185A/Y354A, pH 6.0
0.085
p-phenylenediamine
-
-
0.22
p-phenylenediamine
-
-
0.292
p-phenylenediamine
-
-
0.36
p-phenylenediamine
-
-
0.64
p-phenylenediamine
-
-
0.78 - 2.5
p-phenylenediamine
-
-
0.9
p-phenylenediamine
-
-
1.1
p-phenylenediamine
-
-
1.12
p-phenylenediamine
-
-
1.19
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
-
-
0.036
m-phenylenediamine
-
-
additional information
additional information
P02794
stopped-flow kinetics and initial velocities of iron oxidation of wild-type and mutant enzymes, overview
-
additional information
additional information
Q8DL82
iron oxidation and incorporation kinetics, overview
-
additional information
additional information
-
steady-state kinetics of iron mineralization and of Fe(II) oxidation and thermodynamics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics and steady-state turnover of Fe2+, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22.15
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulphonic acid
-
pH 5.5, 30C
-
0.48
4-phenylenediamine
-
pH 5, 20C
0.038
Cu+
-
pH 5.5, 30C, mutant containing a deleted methionine-rich C-terminal tail
0.155
Cu+
-
pH 5.5, 30C, wild-type
0.375
Cu+
-
pH 5.0
1.3
Cu+
-
pH 5.0
15.8
Cu+
-
Cu+ oxidation, pH 5, 23C, wild-type
0.232
Fe(II)
-
mutant E185A/D409A, pH 6.0
0.405
Fe(II)
-
mutant E185A, pH 6.0
0.66
Fe(II)
-
wild-type, pH 6.0
0.805
Fe(II)
-
mutant D409A, pH 6.0
1.26
Fe(II)
-
mutant D283A, pH 6.0
6.08
Fe(II)
-
mutant D409A, pH 6.0
0.07
Fe2+
-
recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication
0.3
Fe2+
-
pH 5, 20C
0.48
Fe2+
-
mutant E185A, pH 6.0
0.5
Fe2+
-
mutant D278A, pH 6.0
0.505
Fe2+
-
pH 5.0
0.52
Fe2+
-
mutant E185A/Y354A, pH 6.0
0.55
Fe2+
-
mutant E185D, pH 6.0
0.56
Fe2+
-
mutant Y354A, pH 6.0
0.68
Fe2+
-
mutant Y354F, pH 6.0
0.74
Fe2+
-
recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication
0.78
Fe2+
-
wild-type, pH 6.0
1.06
Fe2+
-
pH 5.0
1.06
Fe2+
-
recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication
1.7
Fe2+
-
Fe2+ oxidation, pH 5, 23C, mutant M358S/M361S/M362S/M364S/M366S/M368S
3.91
Fe2+
-
Fe2+ oxidation, pH 5, 23C, wild-type
0.39
hydroquinone
-
mutant E185A, pH 6.0
0.52
hydroquinone
-
mutant E185A/Y354A, pH 6.0
0.62
hydroquinone
-
mutant D278A, pH 6.0
0.85
hydroquinone
-
wild-type, pH 6.0
1.53
hydroquinone
-
mutant E185A, pH 6.0
1.57
hydroquinone
-
mutant E185D, pH 6.0
1.7
hydroquinone
-
mutant Y354F, pH 6.0
2.2
hydroquinone
-
wild-type, pH 6.0
2.3
hydroquinone
-
mutant E185A/D409A, pH 6.0
2.33
hydroquinone
-
mutant D409A, pH 6.0
2.81
hydroquinone
-
mutant D283A, pH 6.0
7.2
hydroquinone
-
mutant Y354A, pH 6.0
0.37
p-phenylenediamine
-
mutant E185A/Y354A, pH 6.0
0.62
p-phenylenediamine
-
mutant D278A, pH 6.0
0.92
p-phenylenediamine
-
wild-type, pH 6.0
0.98
p-phenylenediamine
-
mutant E185A, pH 6.0
1.18
p-phenylenediamine
-
mutant Y354F, pH 6.0
1.73
p-phenylenediamine
-
mutant E185D, pH 6.0
4.8
p-phenylenediamine
-
mutant Y354A, pH 6.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000039
Cu+
-
pH 5.5, 30C, wild-type
0.00008
Cu+
-
pH 5.5, 30C, mutant containing a deleted methionine-rich C-terminal tail
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.25
Q61147
in an Erel assay measuring loss of Fe2+
0.28
-
-
0.29
-
p-phenylenediamine as substrate
0.3
Q61147
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
1.25
-
-
1.25
-
in a transferrin assay measuring transformation of apotransferrin to holotransferrin
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
LITERATURE
5 - 5.2
-
schizophrenics
5
-
o-dianisidine as substrate
5
-
assay at
5
-
assay at
5.5 - 5.6
-
normal persons
5.7
-
phosphate buffer
5.8
-
p-phenylenediamine as substrate
6.5
-
most active in 0.2 M acetate buffer
6.8
-
-
7
P02794
assay at
7.4
-
xanthine oxidoreductase with ferroxidase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
-
-
6 - 8
-
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
Q8DL82
standard assay at
20
-
assay at
22 - 25
-
assay at
23
-
assay at
25
P02794
assay at
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
Q8DL82
assay range
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
retroplacental blood
Manually annotated by BRENDA team
-
venous blood 8
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
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
-
intestinal enterocyte
Manually annotated by BRENDA team
-
vascular epithelial cell
Manually annotated by BRENDA team
-
both hypoxia and CuCl2 increase ceruloplasmin mRNA levels in hepatoma cells due to transcriptional induction of enzyme gene promoter
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
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
nephrotic urine
Manually annotated by BRENDA team
additional information
-
ceruloplasmin protein is not detected in pyramidal cells and granulosa cells of cortex and hippocampus
Manually annotated by BRENDA team
additional information
-
HD103, a clinical isolate obtained from gastrointestinal biopsy specimens of a patient with duodenal ulcer
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
I6WZK7
MmcO is membrane associated, possibly through a lipidation site at cysteine 35
Manually annotated by BRENDA team
-
MmcO is membrane associated, possibly through a lipidation site at cysteine 35
-
Manually annotated by BRENDA team
-
Fet31 and Fet34, both localize to the yeast plasma membrane
Manually annotated by BRENDA team
-
Fet3p has 11 crystallographically mapped N-linked core glycan units. Assembly of four of these units is specifically required for localization of Fet3p to the plasma membrane. Fet3 protein lacking any one of these glycan units is found in an intracellular high-molecular mass species, overview
Manually annotated by BRENDA team
Q8DL82
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
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 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)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
-
SDS-PAGE; SDS-PAGE, apo-CueO
728744
56000
I6WZK7
Western blot
727771
61800
-
protein characterization
438029
72400
-
calculated from amino acid sequence
438029
72870
-
electrospray mass spectrometry
438029
85000
-
-
438029
85000
-
SDS-PAGE
438029
85000
-
holoceruloplasmin, SDS-PAGE
438032
85000
-
-
438032
100000 - 150000
-
glycerol gradient
438028
100000 - 200000
-
gel filtration
438007
100000
-
2 differentially glycosylated forms, SDS-PAGE
438028
113000
-
amino acid composition
438024
114900
-
-
438024
114900
-
amino acid composition
438024
115000
-
human ceruloplasmin antibody reaction
438027
120000
-
2 differentially glycosylated forms, SDS-PAGE
438028
120000
-
recombinant ceruloplasmin
438031
121000
-
amino acid composition
438024
121300
-
gel filtration
438024
123000
-
sedimentation-velocity
438010
124000
-
nonproteolyzed single-chain, sedimentation equilibrium
438006
124000
-
-
438006
124000
-
-
438010
124000
-
gel filtration
438015
124000
-
-
438015
125000
-
amino acid composition
438010
129000
-
determination of peptide chain length
438008
130000
-
-
438008
130000
-
gel filtration, sedimentation equilibrium centrifugation
438016
130000
-
-
438024
130000
-
-
438031
131000
-
sedimentation equilibrium
438008
132000
-
-
438006
132000
-
crystallographic investigation
438008
132000
-
amino acid sequence
438009
132000
-
-
438021, 438022, 438024, 438026, 438027, 438029
133000
-
-
438008, 438015
134000
-
nonproteolyzed single-chain, sedimentation equilibrium
438006
134000
-
form I, meniscus depletion sedimentation equilibrium
438008
135000
-
undegraded single-chain protein, gel filtration, analytical SDS-PAGE
438009
135000
-
human ceruloplasmin antibody reaction
438027
135000
-
apoprotein, SDS-PAGE
438032
137000
-
gel filtration
438008
140000
-
nonreducing SDS-PAGE
438023
145000
-
-
438026
150000
-
-
438006
150000
-
-
438008
155000
-
sedimentation equilibrium
438008
158000
-
sedimentation velocity experiments
437997
160000
-
-
438002
160000
-
light scattering
438003
160000
-
-
438006, 438008
200000
-
human ceruloplasmin antibody reaction
438027
800000 - 2000000
-
ferroxidase II, gel filtration
438002
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24-mer
-
advanced protein assay
24-mer
P0ABD3
BFR consists of 24 identical subunits arranged as 12 subunit dimers, each dimer contains a ferroxidase center, X-ray diffraction
?
-
x * 130000, SDS-PAGE
?
-
x * 129600, MALDI-TOF of recombinant glycoprotein, x * 143000, SDS-PAGE of recombinant protein, x * 121000, SDS-PAGE of PNGase F-treated protein
dimer
-
1 * 17000 + 1 * 59000, 1 * 24000 + 1 * 93000, cleaved by protease
dimer
Q7CN02
Dps proteins structure comparisons, overview
dodecamer
Q99YU7
bending magnet macromolecular crystallography
dodecamer
Q8DL82
12 * 20900, about, sequence calculation, three-dimensional structure analysis of DspA-Te, the subunits forming the pores at the ferritin-like interfaces have a slightly different orientation with respect to the three-fold symmetry axes than in the other Dps structures, overview. DpsA-Te ferroxidase center is unique, owing to the presence of a His78 in place of the canonical Asp metal ligand
monomer
-
-
monomer
-
1 * 130000, SDS-PAGE
monomer
-
1 * 140000, SDS-PAGE
tetramer
-
-
tetramer
-
1 * 19000 + 1 * 25000 + 1 * 26000 + 1 * 67000, SDS-PAGE
tetramer
-
2 * 16000 + 2 * 35000, SDS-PAGE
tetramer
-
1 * 50000 + 1 * 90000 + 1 * 50000, SDS-PAGE
tetramer
-
2 * 16000 + 2 * 59000, SDS-PAGE, 2 * 15900 + 2 * 58900, SDS-PAGE
trimer
-
1 * 18650 + 1 * 50000 + 1 * 70000, limited proteolysis
trimer
-
1 * 19000 + 1 * 50000 + 1 * 67000, limited proteolysis
monomer
-
1 * 121300, SDS-PAGE
additional information
-
ceruloplasmin forms a 1:1 complex with lactoferrin. Complex formation occurs without major conformational rearrangements of either protein
additional information
P02794
three-dimensional structural analysis of wild-type and mutant H ferritins, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
only bi- and triantennary N-glycosidic glucans
glycoprotein
-
carbohydrate content of 7.7%, no high mannose oligosaccharides
glycoprotein
-
glycosylation occurs at N-linked Asn residues 27, 74, 88, 198, 244, 265, 292, 300, or 381, or at the putative O-linked T307 in native soluble sFet3p. Fet3p has 11 crystallographically mapped N-linked core glycan units. Assembly of four of these units is specifically required for localization of Fet3p to the plasma membrane. Core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of the ferritin at 2.1 and 2.7 A resolution for the native and iron bound proteins, respectively. X-ray crystallographic data indicate that the metal ion binding mode, secondary and tertiary structure of the enzyme closely resemble those of bacterial and eukaryotic H-type ferritins. However, the tetrahedral quarternary structure of the enzyme is unprecedented in its symmetry and in the presence of four large pores in the ferritin shell
O29424
crystal structure of CueO is shown at 1.1 A with the 45-residue methionine-rich segment fully resolved, revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a C-terminal highly mobile segment rich in methionine and histidine residues. Crystal structure of the C500S mutant protein is determined in the presence of either Cu(II) or Cu(I)
-
crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC), indicating that HP-NAP can store zinc and cadmium ions in addition to iron ions. Another zinc ion is found inside of the negatively-charged 3fold-related pore, as an iron ion in the iron-containing form, and therefore the pore is suitable for metal ions to pass through
G1UIZ2
purified recombinant H ferritin, 10 mg/ml protein in 10 mM Tris,HCl, pH 7.5, and 0.15 M NaCl, is mixed at equal volumes with crystallization solution containing 0.1 M BICINE-Na, pH 9.0, and 1.9-2.0 M MgCl2, 20C, 1 week, X-ray diffraction structure determination and analysis at 1.52-1.97 A resolution
P02794
small angel X-ray scattering analysis of the complex with lactoferrin. Ceruloplasmin forms a 1:1 complex with lactoferrin. Complex formation occurs without major conformational rearrangements of either protein
-
in complex with zinc and terbium, at 1.8 A and 2.1 A resolution, respectively. Both ions bind to the ferroxidase center in the same location as iron
P80725
determined at 3 A. The crystallographic data implicate the importance of the extended C-terminal region in the iron entry from the three-fold channels to the ferroxidase centre and making iron more readily accessible for the oxidation
-
crystal structures of iron-loaded frog M ferritin determined by flash freezing crystals soaked for different times in iron(II) solutions under aerobic conditions. These structures provide the first X-ray picture of iron(III) products at the ferroxidase site in higher eukaryotes ferritins
P07798
residues D283, E185, D409 provide a Fe(II) binding site that favors ferric ion thus reducing the reduction potential of the bound Fe(II). Residues E185 and D409 form part of the electron-transfer pathway from the bound Fe(II) to the proteins type I Cu(II)
-
determination of the crystal structure of Streptococcus pyogenes Dpr in iron-free and iron-bound form at 2.0 and 1.93 A resolution, respectively
Q99YU7
purified recombinant Dpr in complex with Zn2+, hanging drop vapour diffusion method, protein in 1 M succinic acid, 5% 2-propanol, and 1% w/v PEG 2000 MME, X-ray diffraction structure determination and analysis at 2.1 A resolution
Q7CN02
purified recombinant getagged DpsA-Te, 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of reservoir solution containing 12% w/v PEG 8000 in 0.1 m MES, pH 6.0, 2 weeks, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement
Q8DL82
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
Q8DL82
at pH 2.0, the enzyme structure is stable at room temperature, but completely and irreversibly degenerates at 75-80C
714969
4.8 - 6.4
-
above pH 5.8 activity progressively decreases
437996
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
holo CueO
728744
30
-
truncated BfrB starts unfolding on exposure to even a very low temperature of 30C whereas the native protein remains almost unaffected till 50C before denaturing rapidly
728550
65
-
above irreversible denaturation process of the protein active site
438017
78
-
enzymatic activity is abolished at 78C
728682
100
Q8DL82
completely stable at pH 3.0-7.0, but complete and irreversibe degeneration at 75-80C
714969
additional information
-
thermal denaturation analysis for wild-type and mutant sFet3 proteins, transition temperatures of 52-74C, overview
716849
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable
-
unusually resistant to aging and proteolysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196C, kept in liquid nitrogen exhibits only minor modifications
-
-20C, storage induced heterogeneity and decrease of the oxidase activity
-
-20C, 3 months
-
4C, 0.5 M sodium phosphate buffer, pH 7.0, retains catalytic activity for at least 3 weeks
-
-20C, 0.5 M phosphate buffer, pH 6.9, concentration of approximately 2.5% without noticeable loss of blue colour during 1 month
-
-20C, A280:A610 ratio increases for several weeks on storage
-
-20C, frozen in liquid nitrogen 0.2% enzyme solution in 0.015 M phosphate buffer, pH 6.9, containing 0.1 M NaCl loses its blue colour completely after 2 weeks storage
-
-90C, when frozen in dry ice and thawed, about 5% of the absorbance at 610 nm is lost, no change in the absorbance at 280 nm
-
4C, 0.1 M Tris buffer, pH 8.0, decomposes into fragments when stored for 36-48 h
-
4C, 0.2% enzyme solution in 0.015 M phosphate buffer, pH 6.9, containing 0.1 M NaCl: the A610/A280 ratio is reduced by approximately 10% in 1 month
-
4C, ferroxidase II, purified enzyme is stable for at least 2 weeks
-
4C, purified enzyme sensitive to storage, no oxidase activity after 4 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using a series of native chromatography steps: hydrophobic interaction, gel filtration, and ion exchange
-
recombinant Fet31 and Fet34 from Saccharomycs cerevisiae by glycosidase EndoH treatment and anion exchange chromatography
-
using concanavalin-A-Sepharose and Q-sepharose
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
after expression in baby hamster kidney cells
-
blood plasma ceruloplasmin was purified by DEAE-Sepharose chromatography
-
non-ceruloplasmin ferroxidase II
-
partially
-
recombinant ceruloplasmin, expressed in Pichia pastoris GS115 his4
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment at 60C for 10 min, followed by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
P02794
blood plasma ceruloplasmin was purified by DEAE-Sepharose chromatography
Q61147
using NH4SO4 precipitation and gel filtration
-
blood plasma ceruloplasmin was purified by DEAE-Sepharose chromatography
-
recombinant FLAG-tagged wild-type and mutants N113A and N194A, treatment with EndoH glycosidase
-
recombinant soluble Fet3p
-
recombinant enzyme from Escherichia coli
Q7CN02
recombinant His-tagged protein from Escherichia coli strain BL21(DE3) by heat treatment at 75C for 10 min, dialysis, anion exchange chromatography, and affinity chromatography, followed by cleavage of the His-tag
Q8DL82
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the mnxDEFG operon construct is expressed without a tag in Escherichia coli by inducing at 17C and loading with 2 mM CuSO4 under microaerobic conditions
-
functional expression of Fet31 and Fet34 C-terminally fused to YFP or CFP in Saccharomyces cerevisiae enzyme ScFet3p-deficient strain plasma membrane, functional complementation. Other Fet proteins, e.g. CaFet33, from Candida albicans fail to complement the Saccharomyces cerevisiae mutant due to false localization at the vacuolar membrane
-
overexpressed via plasmid in Escherichia coli strain BL21-Gold (DE3)
Q93PP9
recombinantly expressed in Sf9 cells using the baculovirus expression system. Recombinant MCO1 is expressed without the von Willebrand factor domains and transmembrane segment, and Arg454 is mutated to alanine to reduce proteolytic cleavage
-
expressed in Escherichia coli to create mutants by site-directed mutagenesis
P0ABD3
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
cDNA clones encoding human CP identified, CP gene mapped to human chromosome 3q21-25 by human-mouse somatic-cell-hybrid analysis
-
expressed in Escherichia coli
-
expressed in expressed in baby hamster kidney cells
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
P02794
fully active recombinant human ceruloplasmin produced in the yeast Pichia pastoris
-
gene sequencing and site-directed mutagenesis
-
expressed in C6 glioma cells
-
attempts to obtain soluble, functional MmcO from a variety of systems and conditions failed. Cleared whole-cell lysates of different strains to characterize the multicopper oxidase activity in Mycobacterium tuberculosis are used
I6WZK7
expressed in Escherichia coli
-
apo- and holo-form of CueO are expressed in Escherichia coli; apo- and holo-form of CueO are expressed in Escherichia coli as His-tagged fusion proteins
-
expression of FLAG-tagged wild-type and mutants N113A and N194A
-
FET3 gene cloned, strain M2 carrying plasmid pDY148 used as expression system, recombinant soluble Fet3p produced in yeast
-
expressed in Escherichia coli
Q99YU7
recombinant expression in Escherichia coli
Q7CN02
gene tll2470 or dpsA-Te, expression as soluble His-tagged protein in Escherichia coli strain BL21(DE3)
Q8DL82
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is upregulated under acid stress at pH 5.0 compared to pH 7.0
-
expression of the mmcO gene is increased by copper
I6WZK7
expression of the mmcO gene is increased by copper
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
C500S mutation results in a colorless protein that presumably lacks the T1 copper and has no catalytic activity. Crystal structures of the C500S mutant protein is determined in the presence of either Cu(II) or Cu(I)
M358S/M361S/M362S/M364S/M366S/M368S
-
Km is largely unchanged between the wildtype and mutant proteins, kcat for Cu(I) oxidase activity decreased 4fold, and Fe(II) oxidase activity 2fold, in the mutant protein
W133F
P0ABD3
protein is lesser sensitive to Fe2+ than wild-type protein
W35F
P0ABD3
fluorescence spectrum is blunted compared to wild-type protein
W35F/W133F
P0ABD3
oxidation of Fe2+ to Fe3+ is slightly reduced
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
P02794
site-directed mutagenesis, the initial velocity of iron oxidization is reduced in the mutant
E140Q
P02794
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
C35A
I6WZK7
putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity
C35A
-
putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity
-
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
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)
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
E185D
-
2.8 atoms of Cu per protein, CD and MCD spectra similar 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
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
D66A
Q99YU7
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
D77A
Q99YU7
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
E81A
Q99YU7
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
H50A
Q99YU7
site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation
H62A
Q99YU7
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
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
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
C486A
I6WZK7
cysteine 486 is required for MmcO activity: C486A mutant fails to restore a MmcO knockout mutant
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 30C whereas the native protein remains almost unaffected till 50C before denaturing rapidly
C486A
-
cysteine 486 is required for MmcO activity: C486A mutant fails to restore a MmcO knockout mutant
-
additional information
-
truncated enzyme with a deleted methionine-rich C-terminal tail region shows a decreased turnover and a slightly lower Km value. Ki (Cu+) value increased compared to wild-type. Catalytic efficacy 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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
expression system is developped producing about 2 mg of purified Bacillus sp. strain PL-12 Mn(II) oxidase per liter of Escherichia coli culture in 5 days
medicine
-
mutations in human ceruloplasmin which result in a loss of activity, cause aceruloplasminemia, a neurodegenerative disease
medicine
-
clinical interest relates to its critical role in the diagnosis of Wilson's disease in serum from patients, marked reduction in serum of patients
medicine
-
homogenous ceruloplasmin with ferroxidase activity for the treatment of aplastic anemics, aplastic anemics have low levels of this enzyme, clinical trials have shown effective in 56% of cases
medicine
-
different forms of normal and pathological ceruloplasmins, increasing ceruloplasmin activity in the blood of schizophrenics
medicine
-
unusual antioxidant property of caeruloplasmin have important implications in vivo for conditions such as rheumatoid joint disease and Wilson's disease, where changes in copper homeostasis, caeruloplasmin and oxygen radicals are known to occur
medicine
-
clinical importance because of its role in iron and copper metabolism and transport
medicine
-
production of monoclonal antibodies for use in diagnostic kits for ceruloplasmin related diseases
medicine
-
in fluid from patients with Parkinson's disease, Alzheimer's disease, and 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
medicine
-
serum ceruloplasmin concentrations of less than 0.20, of 0.14 and 0.10 g per l show positive predictive values of 48.3%, 100%, and 100%, respectively, for Wilson disease, and negative predictive values of 98.7%, 97.1%, and 91.9%, with measurement of ceruloplasmin concentration according to a nephelometric method, in ATP7B genotyped subjects. The diagnostic accuracy for Wilson disease using a serum ceruloplasmin concentration of 0.14 g per l as the local decision threshold is therefore better than using a threshold of 0.20 g per l
medicine
-
Serum transferrin, albuminumin and Zinc concentrations are lower in patients with chronic lymphocytic leukemia while serum alpha-1-acid glycoprotein, ceruloplasmin, copper concentrations, and ceruloplasmin oxidase activity are higher in chronic lymphocytic leukemia patients when compared with the control group. Serum ceruloplasmin level positively correlates with serum ceruloplasmin oxidase activity in patients from the early stage group and in patients with advanced stage
medicine
-
study on children with Henoch-Schnlein purpura. Patients at active stage have significantly higher myeloperoxidase activity, higher ceruloplasmin and total oxidant values than the control. Patiens have significantly lower arylesterase activity and lower free thiol levels. Significantly positive correlations are found between total oxidant status and myeloperoxidase, and total oxidant status and ceruloplasmin at disease onset, whereas a negative correlation is found between myeloperoxidase and thiol during remission
medicine
-
both hypoxia and CuCl2 increase ceruloplasmin mRNA levels in hepatoma cells due to transcriptional induction of enzyme gene promoter
medicine
-
the requirement for a ferroxidase to maintain iron transport activity may explain brain iron overload in patients with aceruloplasminemia
medicine
-
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
nutrition
-
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
medicine
-
after induction of cerebral ischemia by ligating bilateral common carotid arteries, the expression of ceruloplasmin mRNA in the cortex and hippocampus decreases, and the longer the animals experience ischemia, the lower the expression. Iron concentration correlates negatively with ceruloplasmin expression
analysis
-
enzyme can be used in analytical biochemistry, especially for the construction of enzyme sensors, enzymes immobilized in enzyme-containing membranes coating oxygen sensitive electrodes and serve for a specific amperometric determination of their substrates in biological materials