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

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.

SUBMITTER: Antipov E 

PROVIDER: S-EPMC2584688 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature