The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

birA  -  bifunctional biotin-[acetylCoA...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3965, JW3941, bioR, dhbB
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of birA

 

High impact information on birA

 

Biological context of birA

 

Associations of birA with chemical compounds

  • For the several birA mutants examined, there appeared to be no direct correlation between effects on minimum biotin requirement and alterations in repressibility, suggesting a possible dual function for the gene [11].
  • The birA protein has been purified to homogeneity in a three-step process involving chromatography on phosphocellulose and hydroxyapatite columns [7].
  • BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL) [12].

References

  1. Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli. León-Del-Rio, A., Leclerc, D., Akerman, B., Wakamatsu, N., Gravel, R.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Cloning and characterization of the Bacillus subtilis birA gene encoding a repressor of the biotin operon. Bower, S., Perkins, J., Yocum, R.R., Serror, P., Sorokin, A., Rahaim, P., Howitt, C.L., Prasad, N., Ehrlich, S.D., Pero, J. J. Bacteriol. (1995) [Pubmed]
  3. Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure. Solbiati, J., Chapman-Smith, A., Cronan, J.E. J. Biol. Chem. (2002) [Pubmed]
  4. Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains. Polyak, S.W., Chapman-Smith, A., Mulhern, T.D., Cronan, J.E., Wallace, J.C. J. Biol. Chem. (2001) [Pubmed]
  5. Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase. Chapman-Smith, A., Morris, T.W., Wallace, J.C., Cronan, J.E. J. Biol. Chem. (1999) [Pubmed]
  6. Crystallization of the bifunctional biotin operon repressor. Brennan, R.G., Vasu, S., Matthews, B.W., Otsuka, A.J. J. Biol. Chem. (1989) [Pubmed]
  7. Overproduction and rapid purification of the biotin operon repressor from Escherichia coli. Buoncristiani, M.R., Otsuka, A.J. J. Biol. Chem. (1988) [Pubmed]
  8. DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli. Buoncristiani, M.R., Howard, P.K., Otsuka, A.J. Gene (1986) [Pubmed]
  9. Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Tirat, A., Freuler, F., Stettler, T., Mayr, L.M., Leder, L. Int. J. Biol. Macromol. (2006) [Pubmed]
  10. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. McManus, E., Luisi, B.F., Perham, R.N. J. Mol. Biol. (2006) [Pubmed]
  11. Use of bio-lac fusion strains to study regulation of biotin biosynthesis in Escherichia coli. Barker, D.F., Campbell, A.M. J. Bacteriol. (1980) [Pubmed]
  12. A unique biotin carboxyl carrier protein in archaeon Sulfolobus tokodaii. Li, Y.Q., Sueda, S., Kondo, H., Kawarabayasi, Y. FEBS Lett. (2006) [Pubmed]
 
WikiGenes - Universities