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

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dc.contributor.authorAntipov, Eugene-
dc.contributor.authorCho, Art E.-
dc.contributor.authorWittrup, K. Dane-
dc.contributor.authorKlibanov, Alexander M.-
dc.date.accessioned2021-09-09T02:40:04Z-
dc.date.available2021-09-09T02:40:04Z-
dc.date.created2021-06-10-
dc.date.issued2008-11-18-
dc.identifier.issn0027-8424-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/122395-
dc.description.abstractA 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.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherNATL ACAD SCIENCES-
dc.subjectDIRECTED EVOLUTION-
dc.subjectSACCHAROMYCES-CEREVISIAE-
dc.subjectFUNCTIONAL EXPRESSION-
dc.subjectBINDING-SITES-
dc.subjectENZYMES-
dc.titleHighly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method-
dc.typeArticle-
dc.contributor.affiliatedAuthorCho, Art E.-
dc.identifier.doi10.1073/pnas.0809851105-
dc.identifier.scopusid2-s2.0-56649111369-
dc.identifier.wosid000261225600025-
dc.identifier.bibliographicCitationPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.105, no.46, pp.17694 - 17699-
dc.relation.isPartOfPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-
dc.citation.titlePROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-
dc.citation.volume105-
dc.citation.number46-
dc.citation.startPage17694-
dc.citation.endPage17699-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaScience & Technology - Other Topics-
dc.relation.journalWebOfScienceCategoryMultidisciplinary Sciences-
dc.subject.keywordPlusDIRECTED EVOLUTION-
dc.subject.keywordPlusSACCHAROMYCES-CEREVISIAE-
dc.subject.keywordPlusFUNCTIONAL EXPRESSION-
dc.subject.keywordPlusBINDING-SITES-
dc.subject.keywordPlusENZYMES-
dc.subject.keywordAuthordirected evolution-
dc.subject.keywordAuthorenzyme design-
dc.subject.keywordAuthormolecular modeling-
dc.subject.keywordAuthorredox enzymes-
dc.subject.keywordAuthorstereoselectivity-
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