4.7 Article

Substrate access path-guided engineering of l-threonine aldolase for improving diastereoselectivity

Journal

CHEMICAL COMMUNICATIONS
Volume 58, Issue 59, Pages 8258-8261

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc02644a

Keywords

-

Funding

  1. National Key R&D Program of China [2019YFA0905000]
  2. Postdoctoral fund of Zhejiang Province [ZJ2021055]

Ask authors/readers for more resources

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).

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available