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Literature summary for 2.8.1.6 extracted from

  • Bui, B.T.S.; Benda, R.; Schuenemann, V.; Florentin, D.; Trautwein, A.X.; Marquet, A.
    Fate of the (2Fe-2S)2+ cluster of Escherichia coli biotin synthase during reaction: A Moessbauer characterization (2003), Biochemistry, 42, 8791-8798.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron in a partially purified fraction the presence of a S2- source and Fe2+ converts the predominant [2Fe-2S] into a 1:1 mixture of [2Fe-2S] and [4Fe-4S], reduced [4Fe-4S] is involved in mediating the cleavage of S-adenosylmethionine and reduced [2Fe-2S] is the sulfur source of biotin Escherichia coli
Iron presence of a [2Fe-2S] cluster Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dethiobiotin + sulfur Escherichia coli catalyzes the last step of the biosynthesis of biotin biotin
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dethiobiotin + sulfur
-
Escherichia coli biotin
-
?
dethiobiotin + sulfur catalyzes the last step of the biosynthesis of biotin Escherichia coli biotin
-
?