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

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

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Flow Cytometry / methods*
  • Horseradish Peroxidase / chemistry*
  • Models, Molecular
  • Mutant Proteins / chemistry*
  • Oxidation-Reduction
  • Saccharomyces cerevisiae
  • Solubility
  • Stereoisomerism
  • Substrate Specificity
  • Surface Properties

Substances

  • Mutant Proteins
  • Horseradish Peroxidase