1.16.3.1: ferroxidase

This is an abbreviated version!
For detailed information about ferroxidase, go to the full flat file.

Reaction

4 Fe(II) + 4 H+ +

Synonyms

AfFtn, apoferritin, bacterial ferritin, bacterial ferroxidase, bacterioferritin, bacterioferritin B, BFR, BfrB, blue copper oxidase, caeruloplasmin, ceruloplasmin, Cp115, Cp135, Cp200, CT1740, CtFtn, cyto-FOX, cytosolic FOX, DdBfr, Dpr, Dps, Dps protein, Dps-like peroxide resistance protein, Dps-Te, DpsA, DpsA-Te, DspA, EncA, encapsulin, encapsulin A, ferritin, ferro-O2-oxidoreductase, ferro:O2 oxidoreductase, ferroxidase, ferroxidase center of bacterioferritin, ferroxidase I, ferroxidase II, ferroxidase, iron II:oxygen oxidoreductase, Fet3, FET3 gene product, fet3p, FOX1, Ftn, FtnA, H ferritin, H' ferritin, H-chain ferritin, Helicobacter pylori neutrophil-activating protein, hephaestin, HP-NAP, HuHF, human ceruloplasmin form I, human H ferritin, human H-chain ferritin, iron(II): oxygen oxidoreductase, L-ferritin, M ferritin, MaDps, MCO1, MmcO, mnxDEFG, monophenol-o-monoxygenase, More, mouse ceruloplasmin, multicopper ferroxidase, multicopper oxidase, multicopper oxidase 1, multicopper oxidase CueO, multicopper oxidase-1, mushroom tyrosinase, mycobacterial multicopper oxidase, neutrophil-activating protein, non-ceruloplasmin ferroxidase, non-specific DNA-binding protein Dps/ferroxidase, rhHp, rHuHF, Rv0846c, serum ferroxidase, VcDps, VCE_000308, xanthine oxidoreductase

ECTree

     1 Oxidoreductases

         1.16 Oxidizing metal ions

             1.16.3 With oxygen as acceptor

                1.16.3.1 ferroxidase

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Results	in table
10	Activating Compound
21952	AA Sequence
32	Application
1	CAS Registry Number
23	Cloned(Commentary)
31	Crystallization (Commentary)
47479	Disease/ Diagnostics
7	Expression
73	General Information
2	General Stability
59	Inhibitors
164	KM Value [mM]
12	Localization
80	Metals/Ions
103	Molecular Weight [Da]
116	Natural Substrates/ Products (Substrates)
497	Organism
3	Pathway
2130	PDB ID
22	pH Optimum
2	pH Range
2	pH Stability
7	Posttranslational Modification
83	Protein Variants
48	Purification (Commentary)
4	Reaction
3	Reaction Type
166	Reference
126	Source Tissue
17	Specific Activity [micromol/min/mg]
12	Storage Stability
274	Substrates and Products (Substrate)
64	Subunits
159	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
1	Temperature Range [°C]
5	Temperature Stability [°C]
41	Turnover Number [1/s]

Natural Substrates Products

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Natural Substrates Products on EC 1.16.3.1 - ferroxidase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

22 entries

4 Fe2+ + 4 H+ + O2

4 Fe3+ + 2 H2O

3 entries

Fe(II) + 4 H+ + O2

Fe(III) + 2 H2O

3 entries

Fe(II) + H+ + O2

Fe(III) + H2O

Homo sapiens

P00450

-

763224

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

18 entries

additional information

?

-

10 entries

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Acidomyces acidophilus

M9PLY0

-

744437

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Acidomyces acidophilus 26774

M9PLY0

-

744437

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Chlorobaculum tepidum

Q8KBP5

-

746386

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS

Q8KBP5

-

746386

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Halobacterium salinarum

B0R7W1

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Halobacterium salinarum ATCC 29341

B0R7W1

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Homo sapiens

-

-

744016, 745071

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Homo sapiens

P00450

the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance

763026

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Lithobates catesbeianus

-

-

744718, 745442

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Microbacterium arborescens

-

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Myxococcus xanthus

Q1D6H4

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Myxococcus xanthus DK 1622

Q1D6H4

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Pseudomonas aeruginosa

-

-

745442

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Rattus norvegicus

P13635

-

744470

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Rattus norvegicus Wistar

P13635

-

744470

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Saccharomyces cerevisiae

P38993

the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance

763026

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Saccharomyces cerevisiae ATCC 204508

P38993

the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance

763026

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Streptomyces coelicolor

Q9R408

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145

Q9R408

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Thermotoga maritima

Q9WZP2

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Vibrio cholerae

A0A0H3Q5A5

-

746541

-

-

?

4 Fe(II) + 4 H+ + O2

4 Fe(III) + 2 H2O

Vibrio cholerae B33

A0A0H3Q5A5

-

746541

-

-

?

4 Fe2+ + 4 H+ + O2

4 Fe3+ + 2 H2O

Candida albicans

-

-

716270

-

-

?

4 Fe2+ + 4 H+ + O2

4 Fe3+ + 2 H2O

Pyrococcus furiosus

-

-

715667

-

-

?

4 Fe2+ + 4 H+ + O2

4 Fe3+ + 2 H2O

Thermosynechococcus vestitus

Q8DL82

-

714969

-

-

?

Fe(II) + 4 H+ + O2

Fe(III) + 2 H2O

Homo sapiens

P00450

-

763223

-

-

?

Fe(II) + 4 H+ + O2

Fe(III) + 2 H2O

Mycobacterium tuberculosis

I6WZK7

-

763203

-

-

?

Fe(II) + 4 H+ + O2

Fe(III) + 2 H2O

Mycobacterium tuberculosis H37Rv

I6WZK7

-

763203

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Agaricus bisporus

-

-

438019

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Anser sp.

-

-

438024

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Bos taurus

-

-

438010, 438011, 438020, 438024, 438029

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Caretta caretta

-

-

438026

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Equus sp.

-

-

438006, 438010, 438011, 438018

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Gallus sp.

-

-

437997, 438015, 438023, 438024, 438026, 438030

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Homo sapiens

-

-

437996, 437997, 437998, 438000, 438001, 438002, 438003, 438004, 438005, 438006, 438007, 438008, 438009, 438010, 438011, 438012, 438013, 438014, 438015, 438016, 438017, 438020, 438021, 438022, 438024, 438026, 438027, 438028, 438029, 438030

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Homo sapiens

P00450

-

438031, 438033

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Homo sapiens

-

-

438033

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Homo sapiens

-

multicopper oxidase essential for normal iron homeostasis

438032

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Oryctolagus cuniculus

-

-

438006, 438010, 438011

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Ovis aries

-

-

438023, 438026

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Rana sp.

-

-

438006

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Rattus norvegicus

-

-

438005, 438006, 438010, 438015, 438027

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Rattus norvegicus Sprague-Dawley

-

-

438005

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Saccharomyces cerevisiae

-

-

438029, 438032

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Saccharomyces cerevisiae

-

iron acquisition pathway

438028

-

-

?

Fe2+ + H+ + O2

Fe3+ + H2O

Sus scrofa

-

-

437997, 437998, 438003, 438006, 438010, 438011, 438015, 438024, 438025

-

-

?

additional information

?

-

Candida albicans

-

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

716270

-

-

?

additional information

?

-

Helicobacter pylori

-

the non-heme iron-containing ferritin has dual ferroxidase and DNA-binding activities, overview

715402

-

-

?

additional information

?

-

Helicobacter pylori

-

the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity

744474

-

-

?

additional information

?

-

Helicobacter pylori YS39

-

the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity

744474

-

-

?

additional information

?

-

Homo sapiens

-

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

685880

-

-

?

additional information

?

-

Listeria innocua

-

enzyme is involved in conferring peroxide tolerance to the bacterium

672025

-

-

?

additional information

?

-

Mus musculus

-

developmental role of enzyme in nervous system organization

660013

-

-

?

additional information

?

-

Rattus norvegicus

P13635

both in vitro and in vivo ceruloplasmin is able to form the specific complex with lactoferrin, the cationic transferrin of exocrine secretions and secretory granules of neutrophils

744470

-

-

?

additional information

?

-

Rattus norvegicus Wistar

P13635

both in vitro and in vivo ceruloplasmin is able to form the specific complex with lactoferrin, the cationic transferrin of exocrine secretions and secretory granules of neutrophils

744470

-

-

?

additional information

?

-

Streptococcus pyogenes

-

Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface

714028

-

-

?