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Glycosyltransferase and its application to glycodiversification of natural products

Title
Glycosyltransferase and its application to glycodiversification of natural products
Authors
Choi S.H.Kim H.S.Yoon Y.J.Kim D.-M.Lee E.Y.
Ewha Authors
윤여준
SCOPUS Author ID
윤여준scopus
Issue Date
2012
Journal Title
Journal of Industrial and Engineering Chemistry
ISSN
1226-086XJCR Link
Citation
vol. 18, no. 4, pp. 1208 - 1212
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
Glycosyltransferase (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.
DOI
10.1016/j.jiec.2012.01.048
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
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