화학공학소재연구정보센터
홈 로그인 로그아웃 연락처 사이트맵
Journal of Industrial and Engineering Chemistry, Vol.18, No.4, 1208-1212, July, 2012
DOI10.1016/j.jiec.2012.01.048  Export Citation
Glycosyltransferase and its application to glycodiversification of natural products
Sung Hee Choi, Hee Sook Kim1, Yeo Joon Yoon2, Dong-Myung Kim3, and Eun Yeol Lee†
  • Department of Chemical Engineering, Kyung Hee University, Gyeonggi-do 446-701, Republic of Korea
  • 1Department of Food Science and Biotechnology, Kyungsung University, Busan 608-736, Republic of Korea
  • 2Department of Chemistry and Nano Science, Ewha Womans University, Seoul 120-750, Republic of Korea
  • 3Department of Fine Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon 305-764, Republic of Korea
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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.
Keywords:Glycosylation;Glycosyltransferase;Secondary metabolites;Glycosyltransferase-A;Glycosyltransferase-B
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