Journal
CHEMICAL COMMUNICATIONS
Volume 58, Issue 59, Pages 8258-8261Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc02644a
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Funding
- National Key R&D Program of China [2019YFA0905000]
- Postdoctoral fund of Zhejiang Province [ZJ2021055]
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The l-threonine aldolase from Leishmania major was engineered to improve its diastereoselectivity by considering the physico-chemical properties of the substrate access path, leading to significant enhancement in diastereomeric excess (de) value.
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 pi-pi interaction cooperated to improve the diastereoselectivity of the enzyme, with a diastereomeric excess (de) value reaching 96.3%(syn) from 26.8%(syn).
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