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Updated: Jul 8, 2026

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
Published on: March 25, 2020
Inverting the enantioselectivity of a carbonyl reductase via substrate-enzyme docking-guided point mutation
Dunming Zhu1, Yan Yang, Stephanie Majkowicz
1Department of Chemistry, Southern Methodist University, Dallas, Texas 75275, USA. dzhu@smu.edu
Abstract:
Substrate-enzyme docking-guided point mutation of a carbonyl reductase from Sporobolomyces salmonicolor led to mutant enzymes, which reversed the enantiopreference and enhanced the enantioselectivity toward the reduction of para-substituted acetophenones. Such a dramatic change in the enantioselectivity indicates that the 245 residue in the catalytic site plays a critical role in determining the enantioselectivity of these ketone reductions, providing valuable insight into our understanding of how residues involved in substrate binding affect the orientation of bound substrate and thus control the reduction stereoselectivity.
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