Mutational insights into human kynurenine aminotransferase 1: modulation of transamination and β-elimination activities across diverse substrates.

ABSTRACT: Human kynurenine aminotransferase 1 (hKYAT1) plays a crucial role in the transamination of aromatic amino acids and kynurenine. This promiscuous homodimeric enzyme transaminates various amino acids into their corresponding α-keto acids. Additionally, hKYAT1 is known to catalyze the β-elimination of cysteine-S conjugates and cysteine-Se conjugates. In this study, we performed mutational analyses of hKYAT1, targeting its catalytic, ligand-binding, and substrate-binding sites. The transamination activity of 13 mutant variants was systematically evaluated against sixteen different amino acid substrates, including kynurenine, selenomethionine (SeMet), and Se-methylselenocysteine (MSC), as well as for the β-elimination of SeMet and MSC. Our results demonstrate that mutations of residues E27 in t

SUBMITTER: Selvam AK 

PROVIDER: S-EPMC12493182 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature