Within human biology, combinations of regioisomeric motifs of α2,6- or α2,3-sialic acids linked to galactose are frequently observed attached to glycoconjugates. These include glycoproteins and glycolipids, with each linkage carrying distinct biological information and function. Microbial linkage-specific sialidases have become important tools for studying the role of these sialosides in complex biological settings, as well as being used as biocatalysts for glycoengineering. However, currently, there is no α2,6-specific sialidase available. This gap has been addressed herein by exploiting the ability of a Photobacterium sp. α2,6-sialyltransferase to catalyze trans-sialidation reversibly and in a highly linkage-specific manner, acting as a pseudosialidase in the presence of cytidine monophosphate. Selective, near quantitative removal of α2,6-linked sialic acids was achieved from a wide range of sialosides including small molecules conjugates, simple glycan, glycopeptide and finally complex glycoprotein including both linkages.

中文翻译：

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高α2,6-选择性假唾液酸酶的应用

在人类生物学中，经常观察到与半乳糖连接的α2，6-或α2，3-唾液酸的区域异构基序的组合与糖缀合物连接。这些包括糖蛋白和糖脂，每个键携带不同的生物学信息和功能。微生物连锁特异性唾液酸酶已成为研究这些唾液酸苷在复杂生物环境中的作用的重要工具，并已被用作糖工程的生物催化剂。但是，目前尚无可用的α2，6-特异性唾液酸酶。通过利用光细菌的能力已在本文中解决了这一差距。sp。α2,6-唾液酸转移酶可逆地以高度键特异性的方式可逆地催化反唾液酸化，在胞苷一磷酸的存在下充当假唾液酸酶。从广泛的唾液酸中，包括小分子结合物，简单的聚糖，糖肽，最后是包括两个键的复杂糖蛋白，都可以选择性，近乎定量地去除α2,6-连接的唾液酸。