1.16.3.2: bacterial non-heme ferritin
This is an abbreviated version!
For detailed information about bacterial non-heme ferritin, go to the full flat file.
Word Map on EC 1.16.3.2
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1.16.3.2
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ferroxidase
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nanocage
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iron-storage
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ferritin-like
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apoferritin
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bacterioferritins
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h-chains
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nutrition
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environmental protection
- 1.16.3.2
- ferroxidase
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nanocage
-
iron-storage
-
ferritin-like
- apoferritin
- bacterioferritins
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h-chains
- nutrition
- environmental protection
Reaction
2 Fe(II) + + 2 H2O = 2 [FeO(OH)] + 4 H+
Synonyms
bacterial ferritin, bacterioferritin, BFR, BfrB, CjDps, DNA-binding protein from starved cells, Dps protein, DpsA, EcFtnA, ferritin, ferritin A, Ftn, FtnA, HuHF, L-ferritin, M ferritin, non-cytochrome ferritin, non-heme bacterial ferritin, non-heme ferritin, non-heme type bacterial ferritin, nonheme bacterial ferritin, nonheme FtnA
ECTree
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Engineering
Engineering on EC 1.16.3.2 - bacterial non-heme ferritin
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H25G
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
H25G/H37G
site-directed mutagenesis, the mutant shows reduced activity to accumulate iron in its inner cavity compared to the wild-type enzyme
H37G
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
H25G
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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
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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
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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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E126A
E130A
E17A
E49A
E94A
H53A
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
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
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
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
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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
E126A
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein. The C-site variants (particularly E49A and E126A) fully regenerate their initial ferroxidase activity within a few hours compared to a day or so required for wild-type EcFtnA
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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
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein
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the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
E17A
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4
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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
E49A
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein. The C-site variants (particularly E49A and E126A) fully regenerate their initial ferroxidase activity within a few hours compared to a day or so required for wild-type EcFtnA
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the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
E94A
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4
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the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
H53A
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4