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

Aadat  -  aminoadipate aminotransferase

Rattus norvegicus

Synonyms: 2-aminoadipate aminotransferase, 2-aminoadipate transaminase, AadAT, Alpha-aminoadipate aminotransferase, KAT/AadAT, ...
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.

High impact information on Aadat


Biological context of Aadat

  • However, bovine kidney AadAT differed from rat kidney AadAT in substrate specificity, amino acid composition and stability when stored [2].
  • CONCLUSIONS: This study demonstrated that retrograde transfer of specific ODN into RGC is feasible and induces downregulation of KAT II cellular expression [3].
  • We describe a new method for downregulating cellular KAT II expression via transfection of RGC by retrograde transfer of ODN [3].

Anatomical context of Aadat


Associations of Aadat with chemical compounds


Other interactions of Aadat


Analytical, diagnostic and therapeutic context of Aadat


  1. Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney. Buchli, R., Alberati-Giani, D., Malherbe, P., Köhler, C., Broger, C., Cesura, A.M. J. Biol. Chem. (1995) [Pubmed]
  2. Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney. Deshmukh, D.R., Mungre, S.M. Biochem. J. (1989) [Pubmed]
  3. A selective method for transfection of retinal ganglion cells by retrograde transfer of antisense oligonucleotides against kynurenine aminotransferase II. Thaler, S., Rejdak, R., Dietrich, K., Ladewig, T., Okuno, E., Kocki, T., Turski, W.A., Junemann, A., Zrenner, E., Schuettauf, F. Mol. Vis. (2006) [Pubmed]
  4. Regulation of oxidative degradation of L-lysine in rat liver mitochondria. Scislowski, P.W., Foster, A.R., Fuller, M.F. Biochem. J. (1994) [Pubmed]
  5. Purification and properties of alpha-aminoadipate aminotransferase from rat liver and kidney mitochondria. Mawal, M.R., Mukhopadhyay, A., Deshmukh, D.R. Prep. Biochem. (1991) [Pubmed]
  6. Alpha-aminoadipate and kynurenine aminotransferase activities from rat kidney. Evidence for separate identity. Mawal, M.R., Deshmukh, D.R. J. Biol. Chem. (1991) [Pubmed]
  7. Some metabotropic glutamate receptor ligands reduce kynurenate synthesis in rats by intracellular inhibition of kynurenine aminotransferase II. Battaglia, G., Rassoulpour, A., Wu, H.Q., Hodgkins, P.S., Kiss, C., Nicoletti, F., Schwarcz, R. J. Neurochem. (2000) [Pubmed]
  8. L-cysteine sulphinate, endogenous sulphur-containing amino acid, inhibits rat brain kynurenic acid production via selective interference with kynurenine aminotransferase II. Kocki, T., Luchowski, P., Luchowska, E., Wielosz, M., Turski, W.A., Urbanska, E.M. Neurosci. Lett. (2003) [Pubmed]
  9. Comparison of lysine and tryptophan catabolizing enzymes in rat and bovine tissues. Mukhopadhyay, A., Mungre, S.M., Deshmukh, D.R. Experientia (1990) [Pubmed]
  10. Kynurenine aminotransferase and alpha-aminoadipate aminotransferase: III. Evidence for identity with halogenated tyrosine aminotransferase. Tobes, M.C., Mason, M. Life Sci. (1978) [Pubmed]
  11. Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferase. Takeuchi, F., Otsuka, H., Shibata, Y. Biochim. Biophys. Acta (1983) [Pubmed]
WikiGenes - Universities