kynurenine-oxoglutarate transaminase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. [EC:2.6.1.7]

Kynurenine-oxoglutarate transaminase activity catalyzes the transfer of an amino group from L-kynurenine to α-ketoglutarate. This reaction is a key step in the kynurenine pathway, which is the major route of tryptophan catabolism in mammals. The enzyme utilizes pyridoxal phosphate (PLP) as a cofactor. In the catalytic cycle, L-kynurenine binds to the active site of the enzyme and forms a Schiff base with PLP. The amino group of L-kynurenine is then transferred to the α-ketoglutarate, forming L-glutamate and α-amino-β-carboxymuconate-ε-semialdehyde. The latter compound is further metabolized to quinolinate, which is a precursor for NAD biosynthesis. Kynurenine-oxoglutarate transaminase activity plays a crucial role in the regulation of tryptophan metabolism and in the production of essential metabolites such as NAD. Dysregulation of this activity has been linked to several human diseases, including neurodegenerative disorders and cancer.'
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Proteins (3)

Compounds (5)