Information on EC 1.16.3.2 - bacterial non-heme ferritin

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

EC NUMBER
COMMENTARY hide
1.16.3.2
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RECOMMENDED NAME
GeneOntology No.
bacterial non-heme ferritin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 Fe(II) + H2O2 + 2 H2O = 2 [FeO(OH)] + 4 H+
show the reaction diagram
(1b)
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2 Fe(II) + O2 + 4 H2O = 2 [FeO(OH)] + 4 H+ + H2O2
show the reaction diagram
(1a)
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4 Fe(II) + O2 + 6 H2O = 4 [FeO(OH)] + 8 H+
show the reaction diagram
overall reaction
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SYSTEMATIC NAME
IUBMB Comments
Fe(II):oxygen oxidoreductase ([FeO(OH)]core-producing)
Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. Thousands of mineralized iron atoms are stored within the core of the structure. The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the major iron-storage protein ferritin A in Escherichia coli acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stress. The iron stored in ferritin A can be retrieved by an iron chaperon IscA for the re-assembly of the iron-sulfur cluster in a proposed scaffold IscU in the presence of the thioredoxin reductase system which emulates normal intracellular redox potential
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Fe(II) + H2O2 + H2O
[FeO(OH)] + H+
show the reaction diagram
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-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+
show the reaction diagram
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
show the reaction diagram
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-
-
-
?
additional information
?
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although H2O2 is a product of dioxygen reduction in FtnA and oxidation occurs with a stoichiometry of Fe2+/O2 about 3:1 most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe2+/H2O2 stoichiometry, thus suppressing hydroxyl-radical formation
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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
Fe(II) + H2O2 + H2O
[FeO(OH)] + H+
show the reaction diagram
-
-
-
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?
Fe(II) + O2 + H2O
[FeO(OH)] + H+
show the reaction diagram
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
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although H2O2 is a product of dioxygen reduction in FtnA and oxidation occurs with a stoichiometry of Fe2+/O2 about 3:1 most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe2+/H2O2 stoichiometry, thus suppressing hydroxyl-radical formation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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isoelectric focusing
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
291500
gel filtration
465000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24-mer
dodecamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apoenzyme as well as enzyme bound to Fn2+ and bound to Zn2+, microdialysis against 20 mM piperazine/HCl buffer at pH 5.2 containing 1 mM EDTA and NaCl concentrations between 0.1 and 0.6 M, at 20°C
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microdialysis against 20 mM piperazine/HCl (pH 5.2)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephacryl S300 gel filtration
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DEAE resin column chromatography and Sephacryl S-300-HR gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JRG2157 cells
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expressed in Escherichia coli JRG2449 cells
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expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the presence of diamide and potassium ferrycianide, enzyme expression is upregulated 5-12fold
in the presence of diamide and potassium ferrycianide, enzyme expression is upregulated 5-12fold; in the presence of diamide and potassium ferrycianide, enzyme expression is upregulated 5-12fold; in the presence of diamide and potassium ferrycianide, enzyme expression is upregulated 5-12fold
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E126A
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the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein
E130A
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the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein
E17A
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the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
E49A
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the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein
E94A
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the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
H53A
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the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
E129C
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the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E129Q
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the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E129R
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the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E130H
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the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E17H
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the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E50H
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the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
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thermostable ferritin can be used in production of clean drinking water and process water. Thermostable ferritin is an excellent system for rapid phosphate and arsenate removal from aqueous solutions down to residual concentrations at the picomolar level
nutrition
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thermostable ferritin can be used in production of clean drinking water and process water. Thermostable ferritin is an excellent system for rapid phosphate and arsenate removal from aqueous solutions down to residual concentrations at the picomolar level
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