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Chemical Compound Review

AC1L978W     6-[2-[3-[[4-[[[(2R,3S,4R,5R)- 5-(6...

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Disease relevance of C01063


High impact information on C01063

  • Analysis of the products showed that this enzyme catalysed the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP [3].
  • Kurthia sp. does not have the bioW gene coding pimeloyl-CoA synthase, suggesting that pimeloyl-CoA may be produced by a different pathway than that of gram-positive bacterium B. subtilis or B. sphaericus, further suggesting a modified fatty acid synthesis pathway via acetyl-CoA instead as E. coli has [4].
  • The bio operon on the acquired symbiosis island of Mesorhizobium sp. strain R7A includes a novel gene involved in pimeloyl-CoA synthesis [5].
  • In addition, the production of pimeloyl-ACP explains the ability of BioI to function as a pimeloyl CoA source in E. coli, which, unlike B. subtilis, is unable to utilize free pimelic acid for biotin production [6].
  • This result strongly suggests that the binding of pimeloyl-CoA induces a conformational change in the active site, and we propose that this new topology is complementary to d-alanine and to the putative reaction intermediate since they both have the same configuration [7].

Chemical compound and disease context of C01063

  • The origin of the carbon atoms of pimeloyl-CoA, the earliest known precursor in the pathway of de novo biotin biosynthesis in Escherichia coli, was investigated by 13C-NMR spectroscopy [8].

Biological context of C01063


  1. Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea. Rodionov, D.A., Mironov, A.A., Gelfand, M.S. Genome Res. (2002) [Pubmed]
  2. Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35. Binieda, A., Fuhrmann, M., Lehner, B., Rey-Berthod, C., Frutiger-Hughes, S., Hughes, G., Shaw, N.M. Biochem. J. (1999) [Pubmed]
  3. Investigation of the first step of biotin biosynthesis in Bacillus sphaericus. Purification and characterization of the pimeloyl-CoA synthase, and uptake of pimelate. Ploux, O., Soularue, P., Marquet, A., Gloeckler, R., Lemoine, Y. Biochem. J. (1992) [Pubmed]
  4. Cloning and characterization of biotin biosynthetic genes of Kurthia sp. Kiyasu, T., Nagahashi, Y., Hoshino, T. Gene (2001) [Pubmed]
  5. The bio operon on the acquired symbiosis island of Mesorhizobium sp. strain R7A includes a novel gene involved in pimeloyl-CoA synthesis. Sullivan, J.T., Brown, S.D., Yocum, R.R., Ronson, C.W. Microbiology (Reading, Engl.) (2001) [Pubmed]
  6. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Stok, J.E., De Voss, J. Arch. Biochem. Biophys. (2000) [Pubmed]
  7. Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies. Ploux, O., Breyne, O., Carillon, S., Marquet, A. Eur. J. Biochem. (1999) [Pubmed]
  8. Origin of carbon atoms of biotin. 13C-NMR studies on biotin biosynthesis in Escherichia coli. Ifuku, O., Miyaoka, H., Koga, N., Kishimoto, J., Haze, S., Wachi, Y., Kajiwara, M. Eur. J. Biochem. (1994) [Pubmed]
  9. Complete sequence and organization of the Serratia marcescens biotin operon. Sakurai, N., Akatsuka, H., Kawai, E., Imai, Y., Komatsubara, S. Microbiology (Reading, Engl.) (1996) [Pubmed]
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