植物尿苷二磷酸糖基转移酶超家族晶体结构

Crystal structures of plant uridine diphosphate-dependent glycosyltransferases

摘要:

糖基转移酶 (Glycosyltransferases, GTs) 催化的糖基化反应几乎是植物中最为重要的反应。GTs家族1中的植物UGTs (UDP-dependent glycosyltransferases) 成员主要运用尿苷二磷酸活化的糖作为糖基供体，因其成员众多、生物功能多样，仅仅通过序列比较和进化分析不能够精确预测其复杂的底物专一性和特有的催化机制，需要后续生化实验的进一步验证。文中主要总结了目前在蛋白结构数据库 (Protein Data Bank, PDB) 中报道的5种植物UGTs的晶体三维结构和定点突变功能研究进展。详细介绍了植物UGTs整体结构的特点以及蛋白与底物相互作用的细节，为更有效地生化定性UGTs以便深入理解底物专一性提供了有力的工具，从而为植物UGTs在酶工程和基因工程中的应用奠定基础。

Abstract:

Glycosyltransferases (GTs) catalyze the transfer of a sugar residue of an activated sugar donor to an acceptor molecule. Many families 1 GTs utilize an uridine diphosphate (UDP) activated sugar as donor in the glycosylation reaction, and most of these belong to a group of GTs referred to as the UGTs. The relationship between the degree of amino acid sequence identity and substrate specificity of the plant UGTs is highly complicated, and the prediction of substrate specificity based on phylogenetic analyses need to be improved by more biochemical characterization. This review summarizes the three dimensional structures of plant UGTs published in the Protein Data Bank (PDB), including the detailed substrate interactions with the sugar and receptor binding pockets and mutational analyses of some critical amino acids. It will be helpful for biochemical characterization the substrate specificity of the individual UGT, and lay the foundation for the enzymatic and genetic manipulation of plant UGTs in the future.