Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Antipov, Eugene | - |
dc.contributor.author | Cho, Art E. | - |
dc.contributor.author | Wittrup, K. Dane | - |
dc.contributor.author | Klibanov, Alexander M. | - |
dc.date.accessioned | 2021-09-09T02:40:04Z | - |
dc.date.available | 2021-09-09T02:40:04Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2008-11-18 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/122395 | - |
dc.description.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. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.subject | DIRECTED EVOLUTION | - |
dc.subject | SACCHAROMYCES-CEREVISIAE | - |
dc.subject | FUNCTIONAL EXPRESSION | - |
dc.subject | BINDING-SITES | - |
dc.subject | ENZYMES | - |
dc.title | Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Cho, Art E. | - |
dc.identifier.doi | 10.1073/pnas.0809851105 | - |
dc.identifier.scopusid | 2-s2.0-56649111369 | - |
dc.identifier.wosid | 000261225600025 | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.105, no.46, pp.17694 - 17699 | - |
dc.relation.isPartOf | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 105 | - |
dc.citation.number | 46 | - |
dc.citation.startPage | 17694 | - |
dc.citation.endPage | 17699 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | DIRECTED EVOLUTION | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | FUNCTIONAL EXPRESSION | - |
dc.subject.keywordPlus | BINDING-SITES | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordAuthor | directed evolution | - |
dc.subject.keywordAuthor | enzyme design | - |
dc.subject.keywordAuthor | molecular modeling | - |
dc.subject.keywordAuthor | redox enzymes | - |
dc.subject.keywordAuthor | stereoselectivity | - |
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