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Literature summary extracted from

  • Lamattina, J.; Nix, D.; Lanzilotta, W.
    Radical new paradigm for heme degradation in Escherichia coli O157:H7 (2016), Proc. Natl. Acad. Sci. USA, 113, 12138-12143.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
2.1.1.342 the [4Fe-4S] cluster of ChuW is extremely oxygen sensitive, and enzyme activity is lost if exposed to any level of molecular oxygen Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.342 Iron contain 3.8 iron atoms per monomer of purified enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.342 2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin Escherichia coli
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.342 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.342 8400
-
 substrate heme, pH not specified in the publication, temperature not specified in the publication Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.342 2 S-adenosyl-L-methionine + heme + 2 reduced flavodoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
 ?
2.1.1.342 2 S-adenosyl-L-methionine + mesoheme + 2 reduced flavodoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
 ?
2.1.1.342 2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
 ?
2.1.1.342 additional information ChuW uses a primary carbon radical to catalyze methyl transfer and rearrangement of the porphyrin ring, resulting in the liberation of iron and opening of the porphyrin ring Escherichia coli ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.342 flavodoxin
-
 Escherichia coli
2.1.1.342 [4Fe-4S]-center purified protein shows a broad absorption feature with a maximum near 400 nm Escherichia coli