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

tyrB  -  tyrosine aminotransferase, tyrosine...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4046, JW4014
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 tyrB

  • The tyrB gene from Escherichia coli K-12 was cloned and sequenced, and the transcriptional start point of tyrB was determined by primer extension [1].
  • Cloning and characterization of the tyrB gene from Salmonella typhimurium [2].

High impact information on tyrB

  • The refined crystallographic structure of the "closed" conformation of chicken mitochondrial aspartate aminotransferase has been used as a template for the construction of models of the two Escherichia coli aminotransferases encoded by the tyrB and aspC genes [3].
  • The tyrB gene was isolated from a cosmid carrying the nearby dnaB gene, identified by its ability to complement a dnaB lesion [4].
  • This conclusion was confirmed by results obtained with combinations of aspC-, tyrB-, and ilvE-deficient mutations in E. coli [5].
  • By using a fusion plasmid in which the lacZ structural gene is transcribed from the tyrB promoter, it was shown that the expression of tyrB is controlled at the transcriptional level by the TyrR protein, with tyrosine as corepressor [1].
  • A comparison between the tyrB operator and those of the other genes belonging to the tyrR regulon is presented [1].

Chemical compound and disease context of tyrB


Biological context of tyrB


Associations of tyrB with chemical compounds


Other interactions of tyrB

  • Comparison of the aspC and tyrB gene sequences reveals that they appear to have diverged as much as is possible within the constraints of functionality and codon usage [4].


  1. Molecular analysis of the regulatory region of the Escherichia coli K-12 tyrB gene. Yang, J., Pittard, J. J. Bacteriol. (1987) [Pubmed]
  2. Cloning and characterization of the tyrB gene from Salmonella typhimurium. Nakai, Y., Hayashi, H., Kagamiyama, H. Biochim. Biophys. Acta (1996) [Pubmed]
  3. Modeling the three-dimensional structures of bacterial aminotransferases. Seville, M., Vincent, M.G., Hahn, K. Biochemistry (1988) [Pubmed]
  4. The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Fotheringham, I.G., Dacey, S.A., Taylor, P.P., Smith, T.J., Hunter, M.G., Finlay, M.E., Primrose, S.B., Parker, D.M., Edwards, R.M. Biochem. J. (1986) [Pubmed]
  5. Remnants of an ancient pathway to L-phenylalanine and L-tyrosine in enteric bacteria: evolutionary implications and biotechnological impact. Bonner, C.A., Fischer, R.S., Ahmad, S., Jensen, R.A. Appl. Environ. Microbiol. (1990) [Pubmed]
  6. Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12. Chao, Y.P., Lai, Z.J., Chen, P., Chern, J.T. Biotechnol. Prog. (1999) [Pubmed]
  7. Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. Gelfand, D.H., Steinberg, R.A. J. Bacteriol. (1977) [Pubmed]
  8. Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Kuramitsu, S., Inoue, K., Ogawa, T., Ogawa, H., Kagamiyama, H. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
WikiGenes - Universities