kynurenine + 2-oxoglutarate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + glutamate

Stable Identifier
Homo sapiens
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AADAT dimer localized in the mitochondrial matrix catalyzes the reaction of kynurenine and 2-oxoglutarate to form 4-(2-aminophenyl)-2,4-dioxobutanoate and glutamate (Han et al. 2008). Biochemical studies of kynurenine transamination in vitro invariably measure kynurenic acid, not 4-(2-aminophenyl)-2,4-dioxobutanoate, the expected transamination product. As noted by Miller et al. (1953), "The keto acid assumed to be formed prior to ring closure in the conversion of kynurenine to kynurenic acid has not yet been detected. In principle, such detection should be possible, since it is sufficiently stable to have been synthesized. It also remains to be established whether ring closure is spontaneous, enzymatic, or both. The formation of kynurenic acid from L-kynurenine by the L-amino acid oxidase of Neurospora suggests, however, that ring closure can be spontaneous, unless the somewhat improbable assumption is made that Neurospora filtrate contained the ring-closing enzyme."

Literature References
PubMed ID Title Journal Year
18056995 Crystal structure of human kynurenine aminotransferase II

Robinson, H, Li, J, Han, Q

J Biol Chem 2008
13069505 The transamination of kynurenine

Miller, IL, Adelberg, EA, Tsuchida, M

J Biol Chem 1953
Catalyst Activity

kynurenine-oxoglutarate transaminase activity of AADAT dimer [mitochondrial matrix]

Orthologous Events
Cross References
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