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dc.contributor.author윤여준-
dc.date.accessioned2016-08-28T10:08:27Z-
dc.date.available2016-08-28T10:08:27Z-
dc.date.issued2012-
dc.identifier.issn1226-086X-
dc.identifier.otherOAK-8987-
dc.identifier.urihttp://dspace.ewha.ac.kr/handle/2015.oak/222819-
dc.description.abstractGlycosyltransferase (GT) catalyzes the transfer of a sugar moiety to acceptor substrates such as secondary metabolites. The majority of GTs has two structural folds, GT-A and GT-B based on 3-D structural analysis. The limited structural fold diversity is compensated by a highly divergent acceptor binding domain for conferring sufficient substrate promiscuity. Various GTs have been engineered to further enhance the glucose transfer activity and expand substrate promiscuity by error-prone PCR and site-directed mutagenesis. Engineered GT-catalyzed glycosylation will certainly play a key role in the generation of scaffold for new drug discovery and control of drug pharmacokinetics. © 2012 The Korean Society of Industrial and Engineering Chemistry.-
dc.languageEnglish-
dc.titleGlycosyltransferase and its application to glycodiversification of natural products-
dc.typeReview-
dc.relation.issue4-
dc.relation.volume18-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.indexKCI-
dc.relation.startpage1208-
dc.relation.lastpage1212-
dc.relation.journaltitleJournal of Industrial and Engineering Chemistry-
dc.identifier.doi10.1016/j.jiec.2012.01.048-
dc.identifier.wosidWOS:000306164400003-
dc.identifier.scopusid2-s2.0-84862794688-
dc.author.googleChoi S.H.-
dc.author.googleKim H.S.-
dc.author.googleYoon Y.J.-
dc.author.googleKim D.-M.-
dc.author.googleLee E.Y.-
dc.contributor.scopusid윤여준(7402126465)-
dc.date.modifydate20200301081000-
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자연과학대학 > 화학·나노과학전공 > Journal papers
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