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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

Reaction

2 Fe(II) +

H2O2
+ 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

     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.3 With oxygen as acceptor
                1.16.3.2 bacterial non-heme ferritin

Engineering

Engineering on EC 1.16.3.2 - bacterial non-heme ferritin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
-
E126A
E130A
W133F
-
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
-
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
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E129Q
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E129R
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E130H
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E17H
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E50H
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme