Kynurenine Aminotransferase II (human) (rec.) (His)

AdipoGen Life Sciences

Kynurenine Aminotransferase II (human) (rec.) (His)

10

Research Use Only

Kynurenine aminotransferases (KATs) are pyridoxal-5-phosphate-dependent enzymes that catalyze the conversion of L-kynurenine into kynurenic acid, a neuroactive metabolite whose unbalancing is associated with a number of brain disorders. Biochemical and structural investigations revealed that L-kynurenine (L-KYN) recognition by hKAT II is achieved by exploiting structural features that are peculiar of this isoform, thus offering the possibility to select/design inhibitor molecules specifically targeting hKAT II to be used as modulators of kynurenic acid synthesis in the CNS. hKAT II is one of the aminotransferases involved in the pyridoxal 5-phosphate (PLP)-dependent irreversible transamination of L-kynurenine (L-KYN) to kynurenic acid (KYNA) in the central nervous system. When assayed in vitro the protein also displays beta-elimination activity. - Protein. Human full-length KAT II is fused at the N-terminus to a His-tag. Source: E. coli. Endotoxin content: N/A. Liquid. In 50 mM phosphate buffer pH 8.0, containing 50mM sodium chloride and 40microM pyridoxal 5-phosphate (PLP). Purity: >97% (SDS-PAGE). Kynurenine aminotransferases (KATs) are pyridoxal-5-phosphate-dependent enzymes that catalyze the conversion of L-kynurenine into kynurenic acid, a neuroactive metabolite whose unbalancing is associated with a number of brain disorders. Biochemical and structural investigations revealed that L-kynurenine (L-KYN) recognition by hKAT II is achieved by exploiting structural features that are peculiar of this isoform, thus offering the possibility to select/design inhibitor molecules specifically targeting hKAT II to be used as modulators of kynurenic acid synthesis in the CNS. hKAT II is one of the aminotransferases involved in the pyridoxal 5-phosphate (PLP)-dependent irreversible transamination of L-kynurenine (L-KYN) to kynurenic acid (KYNA) in the central nervous system. When assayed in vitro the protein also displays beta-elimination activity.

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41116133