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

来源：

CARBOHYDRATE RESEARCH | 2010年 / 345卷 / 17期

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

页码：2458 / 2463

页数：6

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