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Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17694-9. doi: 10.1073/pnas.0809851105. Epub 2008 Nov 12.

Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method.

Author information

  • 1Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

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.

PMID:
19004779
[PubMed - indexed for MEDLINE]
PMCID:
PMC2584688
Free PMC Article

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