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MetaCyc Enzyme: 8-amino-7-oxononanoate synthase

Gene: bioF Accession Numbers: AT5G04620 (MetaCyc), At5g04620

Species: Arabidopsis thaliana col

Summary:
The cDNA encoding 7-keto-8-aminopelargonic acid/ 8-amino-7-oxononanoate synthase (AtbioF) has been isolated from Arabidopsis thaliana. The enzyme catalyzes the transamination of pimeloyl-CoA (carboxyhexanoyl-CoA) to 8-amino-7-oxononanoate, the entry reaction of the biotin biosynthesis. The enzyme was recombinant expressed in Escherichia coli and its molecular function confirmed by means of functional complementation in a mutant Escherichia coli strain. The monomeric enzyme is a cytosolic protein indicating that the biotin biosynthesis in plants is compartmented [Pinon05].

Molecular Weight of Polypeptide: 52.171 kD (from nucleotide sequence), 52 kD (experimental) [Pinon05 ]

Unification Links: Entrez:AAY82238

Relationship Links: Entrez-Nucleotide:PART-OF:DQ017966

Gene-Reaction Schematic: ?

Gene-Reaction Schematic


Enzymatic reaction of: 8-amino-7-oxononanoate synthase

pimeloyl-CoA + L-alanine + H+ <=> CO2 + 8-amino-7-oxononanoate + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Kinetic Parameters:

Substrate
Km (μM)
Citations
pimeloyl-CoA
1.6
[Pinon05]
L-alanine
1400.0
[Pinon05]


References

Pinon05: Pinon V, Ravanel S, Douce R, Alban C (2005). "Biotin synthesis in plants. The first committed step of the pathway is catalyzed by a cytosolic 7-keto-8-aminopelargonic Acid synthase." Plant Physiol 139(4);1666-76. PMID: 16299174


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Thu Aug 27, 2015, BIOCYC14B.