糖基转移酶中中间体的捕获和保留。
Trapping and retaining intermediates in glycosyltransferases.
机构信息
Department of Structural and Molecular Biology, Structural Glycobiology Laboratory, Molecular Biology Institute of Barcelona (IBMB), Spanish National Research Council (CSIC), Barcelona, Catalonia, Spain.
出版信息
J Biol Chem. 2023 Aug;299(8):105006. doi: 10.1016/j.jbc.2023.105006. Epub 2023 Jul 1.
Glycosyltransferases (GTs) attach sugar molecules to a broad range of acceptors, generating a remarkable amount of structural diversity in biological systems. GTs are classified as either "retaining" or "inverting" enzymes. Most retaining GTs typically use an Si mechanism. In a recent article in the JBC, Doyle et al. demonstrate a covalent intermediate in the dual-module KpsC GT (GT107) supporting a double displacement mechanism.
糖基转移酶（GTs）将糖分子连接到广泛的受体上，在生物系统中产生了大量的结构多样性。GTs 分为“保留”或“反转”酶。大多数保留 GTs 通常使用 Si 机制。在最近发表在 JBC 的一篇文章中，Doyle 等人证明了双模块 KpsC GT（GT107）中的一个共价中间体支持双置换机制。
Zotero 插件