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Literature summary for 2.1.1.342 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
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General Stability

General Stability Organism
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + heme + 2 reduced flavodoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
 ?
2 S-adenosyl-L-methionine + mesoheme + 2 reduced flavodoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
 ?
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
 ?
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

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