High impact information on Aadat

• In the rat, one of the described KAT isoforms has been found to correspond to glutamine transaminase K. In addition, rat kidney alpha-aminoadipate aminotransferase (AadAT) also shows KAT activity [1].
• Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney [1].
• Degenerate oligonucleotides were designed from the amino acid sequences of rat kidney KAT/AadAT tryptic peptides for use as primers for reverse transcription-polymerase chain reaction of rat kidney RNA [1].
• KAT/AadAT appears to be structurally homologous to aspartate aminotransferase in the pyridoxal 5'-phosphate binding domain [1].
• The resulting polymerase chain reaction fragment was used to screen a rat kidney cDNA library and to isolate a cDNA clone encoding KAT/AadAT [1].

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

• Mitochondria, isolated from rats pre-treated with glucagon, exhibited higher activities of L-lysine: 2-oxoglutarate reductase, saccharopine dehydrogenase and 2-aminoadipate aminotransferase [4].
• A selective method for transfection of retinal ganglion cells by retrograde transfer of antisense oligonucleotides against kynurenine aminotransferase II [3].
• These results indicate that AadAT from different subcellular fractions is structurally and immunologically identical [5].
• Using the same affinity column, we purified AadAT activities from rat kidney and liver mitochondria [5].

Associations of Aadat with chemical compounds

• We purified alpha-aminoadipate aminotransferase and kynurenine aminotransferase from rat kidney supernatant fraction to electrophoretic homogeneity by ammonium sulfate fractionation, DEAE-Sephacel, and hydroxylapatite chromatography [6].
• Some metabotropic glutamate receptor ligands reduce kynurenate synthesis in rats by intracellular inhibition of kynurenine aminotransferase II [7].
• L-cysteine sulphinate, endogenous sulphur-containing amino acid, inhibits rat brain kynurenic acid production via selective interference with kynurenine aminotransferase II [8].
• The activities of lysine catabolizing enzymes such as AadAT, lysine alpha-ketoglutarate reductase and saccharopine dehydrogenase in the bovine tissues were significantly lower than those found in rat tissues [9].

Other interactions of Aadat

• Kynurenine aminotransferase and alpha-aminoadipate aminotransferase: III. Evidence for identity with halogenated tyrosine aminotransferase [10].

Analytical, diagnostic and therapeutic context of Aadat

• A mixture of aminoadipate aminotransferase and kynurenine aminotransferase activities obtained after hydroxylapatite chromatography was subjected to affinity chromatography [6].
• Immunohistochemistry showed that both methods of ODN application had a similar effect on downregulation of KAT II expression in RGC [3].
• Elution patterns of alpha-aminoadipate aminotransferase (EC 2.6.1.39) activity were identical with those of kynurenine aminotransferase activity on all column chromatographies [11].

References