Highly L and D Enantioselective Variants of Horseradish Peroxidase Discovered by an Ultrahigh-throughput Selection Method

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2008 Nov 14

PMID 19004779

Citations 18

Authors

Eugene Antipov

Art E Cho

K Dane Wittrup

Alexander M Klibanov

Affiliations

Soon will be listed here.

Abstract

A highly efficient selection method for enhanced enzyme enantioselectivity based on yeast surface display and fluorescence-activated cell sorting (FACS) is developed and validated. Its application to horseradish peroxidase has resulted in enzyme variants up to 2 orders of magnitude selective toward either substrate enantiomer at will. These marked improvements in enantioselectivity are demonstrated for the surface-bound and soluble enzymes and rationalized by computational docking studies.

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