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, Eukaryota

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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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E1WS50, P0CJ83, Q5LBE2
UniProt
Manually annotated by BRENDA team
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Q5LBE2
UniProt
Manually annotated by BRENDA team
Campylobacter jejuni subsp. jejuni serotype O:2
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UniProt
Manually annotated by BRENDA team
Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
show the reaction diagram
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
show the reaction diagram
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
show the reaction diagram
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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-
-
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?
additional information
?
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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
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
show the reaction diagram
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
show the reaction diagram
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
show the reaction diagram
Fe(II) + H2O2 + H2O
[FeO(OH)] + H+
show the reaction diagram
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-
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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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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EcFtnA is a non-heme bacterial ferritin. in addition to the conserved A- and B-sites of the diiron ferroxidase center, EcFtnA has a third iron-binding site (the C-site) that is near the diiron site. Analysis of metal binding sites, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7
Campylobacter jejuni subsp. jejuni serotype O:2
assay at
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
22 - 25
Campylobacter jejuni subsp. jejuni serotype O:2
assay at
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 ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
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
19424
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24 * 19424, calculated from amino acid sequence
25000
12 * 25000, SDS-PAGE
291500
gel filtration
465000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24-mer
dodecamer
multimer
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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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) by thermal treatment and two chromatographic steps
Campylobacter jejuni subsp. jejuni serotype O:2
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
E1WS50, P0CJ83, Q5LBE2
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H25G
Campylobacter jejuni subsp. jejuni serotype O:2
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
H25G/H37G
Campylobacter jejuni subsp. jejuni serotype O:2
site-directed mutagenesis, the mutant shows reduced activity to accumulate iron in its inner cavity compared to the wild-type enzyme
H37G
Campylobacter jejuni subsp. jejuni serotype O:2
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
H25G
Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819
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site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
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H25G/H37G
Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819
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site-directed mutagenesis, the mutant shows reduced activity to accumulate iron in its inner cavity compared to the wild-type enzyme
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H37G
Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819
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site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
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W133F
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the Tyr25 radical spectrum simulated for the radical in the wild-type protein is overlaid with the difference spectrum proposed to originate from the same species in the mutant variant, overview
Y24F
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site-directed mutagenesis, variant Y24F is a kinetically competent protein capable of forming a diFe(III) peroxo complex upon addition of the first 48 Fe(II) to the protein with rate parameters similar to wild-type EcFtnA
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
H54A
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site-directed mutagenesis, the mutant variant exhibits a 20% increase in the initial reaction rate of formation of ferric products with 2 or 4 Fe2+/subunit and higher than 200% with 20 Fe2+/subunit. The increased efficiency of the ferritin reaction induced by this mutation is proposed taking advantage of the comparative sequence analysis of other ferritins
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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