Herein we report a novel and more efficient synthesis of SESBA (5) and an analysis of its inhibitory activity using purified recombinant human KAT II. The data are discussed in light of the crystal structure of human KAT II in complex with its natural substrate l-Kyn (1), and on the basis of conserved and nonconserved residues that feature the sequences of speciesspecific orthologs of KAT II (human, rat, and mouse).
Sequence variants in kynurenine aminotransferase II (KAT II) orthologs determine different potencies of the inhibitor S-ESBA
PELLICCIARI, Roberto;CAROTTI, Andrea;MARINOZZI, Maura;MACCHIARULO, Antonio;
2008
Abstract
Herein we report a novel and more efficient synthesis of SESBA (5) and an analysis of its inhibitory activity using purified recombinant human KAT II. The data are discussed in light of the crystal structure of human KAT II in complex with its natural substrate l-Kyn (1), and on the basis of conserved and nonconserved residues that feature the sequences of speciesspecific orthologs of KAT II (human, rat, and mouse).File in questo prodotto:
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