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Gene Review

bioB  -  biotin synthase

Escherichia coli UTI89

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Disease relevance of bioB


High impact information on bioB


Chemical compound and disease context of bioB


Biological context of bioB

  • The changes at position -15 (with respect to the center of the inverted repeat) cause constitutivity of leftward operon expression and decreased expression of bioB, due to alteration of the -35 region of the rightward promoter [14].
  • A cosmid that complements the bioB insertion was isolated, and the bioB gene was localized to a 2.85-kilobase EcoRI-PstI fragment [1].
  • From the nucleotide sequence of the promoter proximal region of the bioB gene, a 13-oligonucleotide sequence believed to be the early transcription termination site has been located [15].
  • Its deduced amino acid sequence is 35.7% and 31.5% identical to that of the E. coli and Bacillus sphaericus bioB gene products, respectively [3].
  • Nucleotide sequence analysis of this fragment revealed that the bioB gene of B. flavum consists of a 1005 bp open reading frame [3].

Anatomical context of bioB


Associations of bioB with chemical compounds


Analytical, diagnostic and therapeutic context of bioB


  1. Isolation of a Rhodobacter capsulatus bioB mutant and cloning of the bioB gene. Cardin, R.D., Biel, A.J. J. Bacteriol. (1990) [Pubmed]
  2. Leftward transcription in the Escherichia coli bio operon does not require products of the rightward transcript. Kotval, J., Campbell, A., Konopa, G., Szybalski, W. Gene (1982) [Pubmed]
  3. Analysis of the biotin biosynthesis pathway in coryneform bacteria: cloning and sequencing of the bioB gene from Brevibacterium flavum. Hatakeyama, K., Kohama, K., Vertès, A.A., Kobayashi, M., Kurusu, Y., Yukawa, H. DNA Seq. (1993) [Pubmed]
  4. Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli. Kiyasu, T., Asakura, A., Nagahashi, Y., Hoshino, T. J. Bacteriol. (2000) [Pubmed]
  5. MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase. Pierrel, F., Hernandez, H.L., Johnson, M.K., Fontecave, M., Atta, M. J. Biol. Chem. (2003) [Pubmed]
  6. MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro. Birch, O.M., Hewitson, K.S., Fuhrmann, M., Burgdorf, K., Baldwin, J.E., Roach, P.L., Shaw, N.M. J. Biol. Chem. (2000) [Pubmed]
  7. The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines. Tamarit, J., Gerez, C., Meier, C., Mulliez, E., Trautwein, A., Fontecave, M. J. Biol. Chem. (2000) [Pubmed]
  8. Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro. Birch, O.M., Fuhrmann, M., Shaw, N.M. J. Biol. Chem. (1995) [Pubmed]
  9. Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase. Jameson, G.N., Cosper, M.M., Hernández, H.L., Johnson, M.K., Huynh, B.H. Biochemistry (2004) [Pubmed]
  10. Escherichia coli biotin synthase: an investigation into the factors required for its activity and its sulfur donor. Sanyal, I., Gibson, K.J., Flint, D.H. Arch. Biochem. Biophys. (1996) [Pubmed]
  11. Flavodoxin is required for conversion of dethiobiotin to biotin in Escherichia coli. Ifuku, O., Koga, N., Haze, S., Kishimoto, J., Wachi, Y. Eur. J. Biochem. (1994) [Pubmed]
  12. [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase. Duin, E.C., Lafferty, M.E., Crouse, B.R., Allen, R.M., Sanyal, I., Flint, D.H., Johnson, M.K. Biochemistry (1997) [Pubmed]
  13. Further investigation on the turnover of Escherichia coli biotin synthase with dethiobiotin and 9-mercaptodethiobiotin as substrates. Tse Sum Bui, B., Lotierzo, M., Escalettes, F., Florentin, D., Marquet, A. Biochemistry (2004) [Pubmed]
  14. Sequence and properties of operator mutations in the bio operon of Escherichia coli. Barker, D.F., Kuhn, J., Campbell, A.M. Gene (1981) [Pubmed]
  15. Attenuation of transcription of biotin genes in Escherichia coli. Nath, S.K. Can. J. Microbiol. (1988) [Pubmed]
  16. 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]
  17. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Ugulava, N.B., Gibney, B.R., Jarrett, J.T. Biochemistry (2001) [Pubmed]
  18. Iron-sulfur center of biotin synthase and lipoate synthase. Ollagnier-De Choudens, S., Sanakis, Y., Hewitson, K.S., Roach, P., Baldwin, J.E., Münck, E., Fontecave, M. Biochemistry (2000) [Pubmed]
  19. Characterization of the cofactor composition of Escherichia coli biotin synthase. Cosper, M.M., Jameson, G.N., Hernández, H.L., Krebs, C., Huynh, B.H., Johnson, M.K. Biochemistry (2004) [Pubmed]
  20. Observation of the iron-sulfur cluster in Escherichia coli biotin synthase by nanoflow electrospray mass spectrometry. Hernández, H., Hewitson, K.S., Roach, P., Shaw, N.M., Baldwin, J.E., Robinson, C.V. Anal. Chem. (2001) [Pubmed]
  21. Mössbauer studies of Escherichia coli biotin synthase: evidence for reversible interconversion between [2Fe-2S](2+) and [4Fe-4S](2+) clusters. Tse Sum Bui, B., Florentin, D., Marquet, A., Benda, R., Trautwein, A.X. FEBS Lett. (1999) [Pubmed]
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