Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 19004779.
- Also identified by DOI 10.1073/pnas.0809851105 and PMC identifier 2584688.
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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.
Medical subject headings
- Flow Cytometry
- Horseradish Peroxidase
- Mutant Proteins