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Chemical Compound Review:

AG-F-60606 8-amino-7-oxo-nonanoic acid

Synonyms: AG-K-94962, CHEBI:15830, CTK1D8243, LMFA01060168, AR-1H4347, ...

Hatakeyama, K. et al., Webster, S.P. et al., Pinon, V. et al., Käck, H. et al., Van Arsdell, S.W. et al., et al.

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Disease relevance of C01092

Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies [1].
Complementation studies using an E. coli bioF mutant and a B. subtilis bio112TG3 strain, revealed that the third ORF of this cluster encodes 7-keto-8-aminopelargonic acid synthetase [2].
Three coryneform bacteria, Brevibacterium flavum, Brevibacterium lactofermentum and Corynebacterium glutamicum have been shown to be able to convert 7-keto-8-aminopelargonic acid to biotin through a biotin synthetic pathway identical to that from Escherichia coli (Hatakeyama et al., DNA Sequence, in press, 1993) [3].

High impact information on C01092

Bio5p mediates the transport of 7-keto-8-aminopelargonic acid across the yeast plasma membrane, a compound that is used as a precursor in biotin biosynthesis [4].
The product of the bioF gene, 7-keto-8-aminopelargonic acid synthetase, was found to be similar to 5-aminolevulinic acid synthetase [5].
Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction [6].
In this study, a genomic-based approach allowed us to clone an Arabidopsis (Arabidopsis thaliana) cDNA coding 7-keto-8-aminopelargonic acid (KAPA) synthase, the first committed enzyme of the biotin synthesis pathway, which we named AtbioF [7].
From the structure of the non-productive complex of the holoenzyme with the substrate 7-keto-8-aminopelargonic acid the location of the active site and residues involved in substrate binding have been identified [8].

Associations of C01092 with other chemical compounds

8-Amino-7-oxononanoate synthase (also known as 7-keto-8-aminopelargonate synthase, EC 2.3.1.47) is a pyridoxal 5'-phosphate-dependent enzyme which catalyzes the decarboxylative condensation of L-alanine with pimeloyl-CoA in a stereospecific manner to form 8(S)-amino-7-oxononanoate [9].

Gene context of C01092

In biotin biosynthesis, DAPA aminotransferase encoded by the bioA gene catalyzes the formation of the intermediate 7,8-diaminopelargonic acid (DAPA) from 7-keto-8-aminopelargonic acid (KAPA) [10].
In addition, they were evolutionarily related to 7-keto-8-aminopelargonic acid synthetase (BioF) and 2-amino-3-ketobutyrate coenzyme A ligase (Kbl), enzymes which catalyze similar reactions [11].

References

Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies. Bhor, V.M., Dev, S., Vasanthakumar, G.R., Kumar, P., Sinha, S., Surolia, A. J. Biol. Chem. (2006) [Pubmed]
Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin. Gloeckler, R., Ohsawa, I., Speck, D., Ledoux, C., Bernard, S., Zinsius, M., Villeval, D., Kisou, T., Kamogawa, K., Lemoine, Y. Gene (1990) [Pubmed]
Genomic organization of the biotin biosynthetic genes of coryneform bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium flavum. Hatakeyama, K., Hohama, K., Vertès, A.A., Kobayashi, M., Kurusu, Y., Yukawa, H. DNA Seq. (1993) [Pubmed]
Vhr1p, a New Transcription Factor from Budding Yeast, Regulates Biotin-dependent Expression of VHT1 and BIO5. Weider, M., Machnik, A., Klebl, F., Sauer, N. J. Biol. Chem. (2006) [Pubmed]
The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon. Otsuka, A.J., Buoncristiani, M.R., Howard, P.K., Flamm, J., Johnson, C., Yamamoto, R., Uchida, K., Cook, C., Ruppert, J., Matsuzaki, J. J. Biol. Chem. (1988) [Pubmed]
Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction. Stoner, G.L., Eisenberg, M.A. J. Biol. Chem. (1975) [Pubmed]
Biotin synthesis in plants. The first committed step of the pathway is catalyzed by a cytosolic 7-keto-8-aminopelargonic acid synthase. Pinon, V., Ravanel, S., Douce, R., Alban, C. Plant Physiol. (2005) [Pubmed]
Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes. Käck, H., Sandmark, J., Gibson, K., Schneider, G., Lindqvist, Y. J. Mol. Biol. (1999) [Pubmed]
Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Webster, S.P., Alexeev, D., Campopiano, D.J., Watt, R.M., Alexeeva, M., Sawyer, L., Baxter, R.L. Biochemistry (2000) [Pubmed]
Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction. Van Arsdell, S.W., Perkins, J.B., Yocum, R.R., Luan, L., Howitt, C.L., Chatterjee, N.P., Pero, J.G. Biotechnol. Bioeng. (2005) [Pubmed]
Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes. Neidle, E.L., Kaplan, S. J. Bacteriol. (1993) [Pubmed]

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