Dissecting the mechanism by which glycosyltransferases catalyse mannosyl transfer

剖析糖基转移酶催化甘露糖基转移的机制

• 批准号: BB/E000568/1
• 负责人: David Bolam
• 金额: $ 40.84万
• 依托单位: Newcastle University
• 依托单位国家: 英国
• 项目类别: Research Grant
• 财政年份: 2007
• 资助国家: 英国
• 起止时间: 2007 至 无数据
• 项目状态: 已结题
• 来源: https://gtr.ukri.org/projects?ref=BB%2FE000568%2F1
• 关键词: Dissecting; mechanism; glycosyltransferases; catalyse; mannosyl

The linking of sugars to a variety of different proteins has an important influence on the function of cells. The biological catalysts or enzymes that speed up the reactions in which sugars are linked to other molecules are known as glycosyltransferases. Although these enzymes and are industrially and biologically important, they have not been extensively studied because they are difficult to produce in large amounts. In this project we will take advantage of our ability to produce significant quantities of glycosyltransferases that catalyse the transfer of the sugar mannose onto other molecules. The three dimensional structure of these enzymes will be determined and the information will be used to synthesise inhibitors of these biological catalysts and to use molecular engineering techniques to manipulate their biological properties.

糖与多种不同蛋白质的连接对细胞的功能有重要影响。加速糖与其他分子连接反应的生物催化剂或酶被称为糖基转移酶。尽管这些酶在工业和生物学上都很重要，但由于它们很难大量生产，因此尚未得到广泛的研究。在这个项目中，我们将利用我们生产大量糖基转移酶的能力，催化甘露糖转移到其他分子上。这些酶的三维结构将被确定，这些信息将用于合成这些生物催化剂的抑制剂，并使用分子工程技术来操纵它们的生物特性。

项目成果

Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.

• DOI: 10.1038/nchembio.278
• 发表时间: 2010-02
• 期刊: Nature chemical biology
• 影响因子: 14.8
• 作者: Zhu Y;Suits MD;Thompson AJ;Chavan S;Dinev Z;Dumon C;Smith N;Moremen KW;Xiang Y;Siriwardena A;Williams SJ;Gilbert HJ;Davies GJ
• 通讯作者: Davies GJ

Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidase.

• DOI: 10.1371/journal.pone.0009006
• 发表时间: 2010-02-03
• 期刊: PloS one
• 影响因子: 3.7
• 作者: Suits MD;Zhu Y;Taylor EJ;Walton J;Zechel DL;Gilbert HJ;Davies GJ
• 通讯作者: Davies GJ