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Structural highlights

Function

HKT_AEDAE Catalyzes the pyridoxal 5'-phosphate-dependent transamination of both 3-hydroxykynurenine and L-kynurenine to xanthurenic acid and kynurenic acid, respectively, preferentially using the alpha-ketoacid pyruvate, glyoxylate or oxaloacetate as the amino group acceptor (PubMed:11880382, PubMed:12220660). The affinity and catalytic efficiency for 3-hydroxykynurenine is higher than for L-kynurenine (PubMed:12220660). Involved in the detoxification of cytotoxic metabolite 3-hydroxykynurenine generated by the hydroxylation of L-kynurenine, an intermediate in the tryptophan catabolism pathway (PubMed:11880382, PubMed:12220660). Also catalyzes, although with a lesser efficiency, the transamination of alanine with glyoxylate as an amino group acceptor (PubMed:11880382). May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the diet (Probable).^{[1] [2] [3] [4]}

See Also

• Aminotransferase 3D structures

References

1. ↑ Han Q, Fang J, Li J. 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti. J Biol Chem. 2002 May 3;277(18):15781-7. PMID:11880382 doi:10.1074/jbc.M201202200
2. ↑ Han Q, Li J. Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase. FEBS Lett. 2002 Sep 11;527(1-3):199-204. PMID:12220660 doi:10.1016/s0014-5793(02)03229-5
3. ↑ Han Q, Fang J, Li J. 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti. J Biol Chem. 2002 May 3;277(18):15781-7. PMID:11880382 doi:10.1074/jbc.M201202200
4. ↑ Han Q, Li J. Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase. FEBS Lett. 2002 Sep 11;527(1-3):199-204. PMID:12220660 doi:10.1016/s0014-5793(02)03229-5