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Literature summary for 1.16.3.2 extracted from

  • Bitoun, J.P.; Wu, G.; Ding, H.
    Escherichia coli FtnA acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stress (2008), Biometals, 21, 693-703.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Fe(II) + O2 + H2O Escherichia coli
-
[FeO(OH)] + H+ + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fe(II) + O2 + H2O
-
Escherichia coli [FeO(OH)] + H+ + H2O2
-
?

Synonyms

Synonyms Comment Organism
ferritin A
-
Escherichia coli
FtnA
-
Escherichia coli

General Information

General Information Comment Organism
physiological function 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 Escherichia coli