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Literature summary extracted from

  • Dailey, H.A.; Septer, A.N.; Daugherty, L.; Thames, D.; Gerdes, S.; Stabb, E.V.; Dunn, A.K.; Dailey, T.A.; Phillips, J.D.
    The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelatase (2011), mBio, 2, e00248.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.4 Escherichia coli
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.4 additional information holo-YfeX effectively oxidizes both protoporphyrinogen IX and coproporphyrinogen III, see for EC 1.3.3.3, to their corresponding porphyrins Escherichia coli ?
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 ?
1.3.3.4 protoporphyrinogen IX + 3 O2
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 Escherichia coli protoporphyrin IX + 3 H2O2
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 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.4 protein YfeX
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 Escherichia coli
1.3.3.4 YfeX
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 Escherichia coli

General Information

EC Number General Information Comment Organism
1.3.3.4 additional information Vibrio fischeri, an organism that can utilize heme as an iron source when grown under iron limitation, is able to grow with heme as the sole source of iron when its YfeX homolog is absent. Plasmid-driven expression of Escherichia coli YfeX in Vibrio fischeri grown with heme does not result in accumulation of protoporphyrin Escherichia coli
1.3.3.4 physiological function YfeX effectively decolorizes the dyes alizarin red and Cibacron blue F3GA and has peroxidase activity with pyrogallal but not guiacol. YfeX oxidizes protoporphyrinogen to protoporphyrin in vitro. But it shows no dechelation of heme to free porphyrin as purified enzyme or in cellular extracts of Escherichia coli overexpressing YfeX. YfeX is a typical dye-decolorizing peroxidase (or DyP) and not a dechelatase Escherichia coli