The L-threonine aldolase from Leishmania major 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… Click to show full abstract
The L-threonine aldolase from Leishmania major 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%syn from 26.8%syn.
Keywords:
access path;
substrate access;
diastereoselectivity;
threonine aldolase
Journal Title: Chemical communications
Year Published: 2022
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Journal Title: Chemical communications
Year Published: 2022
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!