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dc.contributor.authorKim, MJ-
dc.contributor.authorAhn, Y-
dc.contributor.authorPark, J-
dc.contributor.author박재욱-
dc.date.accessioned2016-03-31T12:57:40Z-
dc.date.available2016-03-31T12:57:40Z-
dc.date.issued2002-12-
dc.identifier.citationCURRENT OPINION IN BIOTECHNOLOGY-
dc.identifier.citationv.13-
dc.identifier.citationno.6-
dc.identifier.citationpp.578-587-
dc.identifier.issn0958-1669-
dc.identifier.other2002-OAK-0000003052-
dc.identifier.urihttps://oasis.postech.ac.kr/handle/2014.oak/18792-
dc.description.abstractThe combination of enzyme and metal catalysis is described as a useful method for the synthesis of optically active compounds. A key feature of this new methodology is the use of metal catalysts for the in situ racemization of enzymatically unreactive enantiomers in the enzymatic resolution of racemic substrates. So far, two combinations - lipase-ruthenium and lipase-palladium - have been developed for the efficient dynamic kinetic resolution of alcohols and amines. The use of these combinations has also been extended to catalysis of the asymmetric transformation of ketones, their enol acetates, and ketoximes. In most cases, enzyme-metal combination catalysis has provided good yields and high optical purities.-
dc.description.statementofresponsibilityX-
dc.publisherCURRENT BIOLOGY LTD-
dc.subjectSECONDARY ALCOHOLS-
dc.subjectENZYMATIC RESOLUTION-
dc.subjectCHIRAL ACETATES-
dc.subjectAMINO ALCOHOLS-
dc.subjectENOL ACETATES-
dc.subjectRACEMIZATION-
dc.subjectLIPASE-
dc.subjectPALLADIUM-
dc.subjectKETONES-
dc.subjectROUTE-
dc.titleDynamic kinetic resolutions and asymmetric transformations by enzymes coupled with metal catalysis-
dc.typeArticle-
dc.contributor.college화학과-
dc.author.googleKim, MJ-
dc.author.googleAhn, Y-
dc.author.googlePark, J-
dc.relation.volume13-
dc.relation.issue6-
dc.relation.startpage578-
dc.relation.lastpage587-
dc.contributor.id10075891-
dc.publisher.locationUK-
dc.relation.journalCURRENT OPINION IN BIOTECHNOLOGY-
dc.relation.indexSCI급, SCOPUS 등재논문-
dc.relation.sciSCI-
dc.collections.nameJournal Papers-
dc.type.docTypeREVIEW-

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