Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method.
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ABSTRACT:
SUBMITTER: Antipov E
PROVIDER: S-EPMC2584688 | biostudies-literature | 2008 Nov
REPOSITORIES: biostudies-literature
Publications
Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method.
Antipov Eugene E Cho Art E AE Wittrup K Dane KD Klibanov Alexander M AM
Proceedings of the National Academy of Sciences of the United States of America 20081112 46
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. ...[more]
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