Acceptor specificity in the transglycosylation reaction using Endo-M

被引:14
作者
Tomabechi, Yusuke [1 ,2 ]
Odate, Yuki [1 ]
Izumi, Ryuko [3 ]
Haneda, Katsuji [1 ]
Inazu, Toshiyuki [1 ,2 ]
机构
[1] Tokai Univ, Sch Engn, Dept Appl Chem, Kanagawa 2591292, Japan
[2] Tokai Univ, Inst Glycosci, Kanagawa 2591292, Japan
[3] Res Assoc Biotechnol, Minato Ku, Tokyo 1050003, Japan
关键词
Endo-beta-N-acetylglucosaminidase; Endo-M; Transglycosylation reaction; Recognition site; BETA-N-ACETYLGLUCOSAMINIDASE; ASPARAGINE-LINKED OLIGOSACCHARIDES; CHEMOENZYMATIC SYNTHESIS; MUCOR-HIEMALIS; GLYCOPROTEINS; ANALOGS; ENDOGLYCOSIDASE; GLYCOSYNTHASES; GLYCOPEPTIDE; GLYCANS;
D O I
10.1016/j.carres.2010.08.022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-beta-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to 6-hydroxy functions of GlcNAc were found to be essential for the transglycosylation reaction using Endo-M. Furthermore, it was determined that Endo-M strictly recognizes a 1,3-diol structure consisting of primary and secondary hydroxyl groups. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2458 / 2463
页数:6
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