Abstract

This chapter provides an overview of the kynurenine aminotransferase from kidney supernatant. L-kynurenine: α-ketoglutarate aminotransferase (cyclizing) activity of rat kidney supernatant, an enzyme in tryptophan catabolism, copurifies with the activity of α-aminoadipate: α-ketoglutarate aminotransferase. The presence of aminoadipate (kynurenine) aminotransferase in kidney represents an enzyme associated with lysine catabolism rather than with tryptophan degradation. α-aminoadipate (kynurenine) aminotransferase also catalyzes aminotransfer of 3,5-diiodotyrosine (halogenated tyrosine aminotransferase) suggesting a possible role in thyroid hormone metabolism. The reactions catalyzed by the kynurenine and halogenated tyrosine aminotransferase activities are presented diagrammatically. α-aminoadipate (kynurenine):α-ketoglutarate aminotransferase activity is also present in rat kidney mitochondria and the supernatant and mitochondrial fractions of rat liver. The activity of the L-α-aminoadipate aminotransferase is measured by the rate of disappearance or appearance of α-ketoglutarate with glutamate dehydrogenase. The chapter also reviews the kynurenine aminotransferase assay. The activity of kynurenine aminotransferase is measured spectrophotometrically by following the appearance of kynurenate.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call