Báo cáo khoa học: Crystal structures of Aedes aegypti kynurenine aminotransferase
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Aedes aegyptikynurenine aminotransferase (AeKAT) catalyzes the irrevers-ible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7-nicotinic acetycholine receptors. Here, we report the crys-tal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 A ˚ , respectively. The structure was solved by a combination of single-wave-length anomalous dispersion and molecular replacement approaches.
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