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

  • Eugene Antipov
  • , Art E. Cho
  • , K. Dane Wittrup
  • , Alexander M. Klibanova

Research output: Contribution to journalArticlepeer-review

43 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)17694-17699
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume105
Issue number46
DOIs
Publication statusPublished - 2008 Nov 18

Keywords

  • Directed evolution
  • Enzyme design
  • Molecular modeling
  • Redox enzymes
  • Stereoselectivity

ASJC Scopus subject areas

  • General

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