Publications by authors named "Lanxin Xiao"
Article Synopsis
- l-threonine aldolase (LTA) is essential for creating important β-hydroxy-α-amino acids used in pharmaceuticals and pesticides, but its limited heat stability restricts industrial use.
- The study focuses on a method to enhance LTA's stability by adjusting its V-shaped subunit's rigidity through modifications far from the active center, overcoming the problem of balancing stability and activity.
- The researchers successfully created a mutant enzyme (G85A/M207L/A12C) that shows a 20°C increase in thermostability and improved enzyme activity, demonstrating the potential for engineering other enzymes with similar structures.
l-threonine aldolase (LTA) catalyzes C-C bond synthesis with moderate diastereoselectivity. In this study, with LTA from Cellulosilyticum sp (CpLTA) as an object, a mutability landscape was first constructed by performing saturation mutagenesis at substrate access tunnel amino acids. The combinatorial active-site saturation test/iterative saturation mutation (CAST/ISM) strategy was then used to tune diastereoselectivity.
View Article and Find Full Text PDFThe L-threonine aldolase from was engineered to improve its diastereoselectivity by a CAST/ISM strategy, providing insights into the relationship between the physico-chemical properties of the substrate access path and diastereoselectivity. The steric hindrance, hydrophobic interaction and π-π interaction cooperated to improve the diastereoselectivity of the enzyme, with a diastereomeric excess (de) value reaching 96.3% from 26.
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