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Literature summary for 2.8.1.6 extracted from

  • Ugulava, N.B.; Frederick, K.K.; Jarrett, J.T.
    Control of adenosylmethionine-dependent radical generation in biotin synthase: A kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB (2003), Biochemistry, 42, 2708-2719.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
S-adenosyl-L-methionine
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron 1 [2Fe-2S] cluster per monomer, but enzyme can be reconstituted to contain an additional [4Fe-4S] cluster, both clusters must be present for tight substrate binding Escherichia coli

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
-
?

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli