期刊
CARBOHYDRATE RESEARCH
卷 430, 期 -, 页码 36-43出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2016.04.012
关键词
Escherichia coli; WclR; Galactosyltransferase; Mass spectrometry
资金
- National 973 Project of China [2012CB721101, 2013CB733904]
- International Science & Technology Cooperation Program of China [2013DFR30640]
- National Natural Science Foundation of China (NSFC) [31530083, 31270003, 81471904, 31371259, 31270133, 31470194]
- Russian Foundation for Basic Research [16-04-00372]
- Special Research Found for the Doctoral Program of Higher Education [20110031110022]
- Project of Tianjin, China [13TXSYJC40100]
- Chinese Ministry of Education [113015A]
Glycosyltransferases (GTs) catalyze the formation of regio- and stereo-specific glycosidic linkages between specific sugar donors and recipients. In this study, the function of the gene wclR from the Escherichia coli O3 O-antigen gene cluster that encodes an a 1, 3-galactosyltransferase (GalT) that acts on the linkage Gal alpha 1, 3-GlcNAc was biochemically characterized. WclR was expressed in E. coli BL21 (DE3), and the enzymatic product was identified by liquid chromatography-mass spectrometry (LC-MS), collision-induced dissociation electrospray ionization ion trap multiple tandem MS (CID-ESI-IT-MSn) and galactosidase digestion, using UDP-Gal as the donor substrate and the synthetic acceptor substrate GlcNAc-PP-De (decyl diphosphate N-acetylglucosamine). The physiochemical properties and the substrate specificity of WclR were investigated. WclR is the first bacterial GalT characterized that acts on the linkage Gal alpha 1, 3-GlcNAc. This study enhanced our knowledge of the diversified functions of GTs and provided a novel enzyme source for possible pharmaceutical application. (C) 2016 Elsevier Ltd. All rights reserved.
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