Related Experiment Video
Updated: Mar 25, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
New Concepts for Increasing the Efficiency in Directed Evolution of Stereoselective Enzymes
Zhoutong Sun1,2, Ylva Wikmark3, Jan-E Bäckvall4
1Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470, Mülheim an der Ruhr, Germany.
Abstract:
Directed evolution of stereo- and regioselective enzymes constitutes a prolific source of catalysts for asymmetric transformations in organic chemistry. In this endeavor (iterative) saturation mutagenesis at sites lining the binding pocket of enzymes has emerged as the method of choice, but uncertainties regarding the question of how to group many residues into randomization sites and how to choose optimal upward pathways persist. Two new approaches promise to beat the numbers problem effectively. One utilizes a single amino acid as building block for the randomization of a 10-residue site, the other also employs only one but possibly different amino acid at each position of a 9-residue site. The small but smart libraries provide highly enantioselective epoxide hydrolase or lipase mutants, respectively.
Related Concept Videos
SN2 Reaction: Stereochemistry
If the substrate is an achiral molecule at the α-carbon, the inversion of configuration is not...
Diels–Alder Reaction Forming Cyclic Products: Stereochemistry
Sharpless Epoxidation
Stereochemical Effects of Enolization
Catalytically Perfect Enzymes
Most enzymes...
Regioselective Formation of Enolates

