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Crystal structure of 3-hydroxykynurenine transaminase from Aedes aegypti
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Structural highlights
FunctionHKT_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 AlsoReferences
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This page was last modified 06:30, 11 October 2023.