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Literature summary for 2.3.1.47 extracted from

  • Alexeev, D.; Alexeeva, M.; Baxter, R.L.; Campopiano, D.J.; Webster, S.P.; Sawyer, L.
    The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme (1998), J. Mol. Biol., 284, 401-419.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
bioF gene overexpression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
pH 8.5-8.9, ammonium sulfate precipitation, apoenzyme, X-ray diffraction structure analysis with and without bound pyridoxyl-5'-phosphate, model, active site residues Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
amino acid sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-carboxyhexanoyl-CoA + L-alanine Escherichia coli i.e. pimeloyl-CoA 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ?
6-carboxyhexanoyl-CoA + L-alanine Escherichia coli reaction in biotin biosynthesis 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P12998
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from E. coli Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein] reaction mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-carboxyhexanoyl-CoA + L-alanine i.e. pimeloyl-CoA Escherichia coli 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ?
6-carboxyhexanoyl-CoA + L-alanine reaction in biotin biosynthesis Escherichia coli 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ?

Subunits

Subunits Comment Organism
More dimer, active site is formed at the interface between the monomers Escherichia coli

Synonyms

Synonyms Comment Organism
AONS
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Escherichia coli