4.6 Article

Improving the Cβ Stereoselectivity of L-Threonine Aldolase for the Synthesis of L-threo-4-Methylsulfonylphenylserine by Modulating the Substrate-Binding Pocket To Control the Orientation of the Substrate Entrance

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Article Biotechnology & Applied Microbiology

A recombinant L-threonine aldolase with high diastereoselectivity in the synthesis of L-threo-dihydroxyphenylserine

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Summary: A new L-Threonine aldolase (L-TA) from black bears' gut microbiota, with an Arg318 mutation, showed significantly improved efficiency and selectivity in synthesizing beta-hydroxy-alpha-L amino acids. Particularly, the mutant provided the best-ever diastereoselectivity in synthesizing L-threo-DOPS, indicating promising potential for enzymatic synthesis of other important amino acids. The study also suggested the crucial role of Arg318 in improving the diastereoselectivity of L-TAs, providing valuable insights for future research.

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