National Glycoengineering Research Center, State Key Laboratory of Microbial Technology , Shandong University , Qingdao 266237 , China.
College of Pharmacy , Nankai University , Tianjin 300071 , China.
J Am Chem Soc. 2019 Mar 20;141(11):4547-4552. doi: 10.1021/jacs.9b00044. Epub 2019 Mar 11.
The first bacterial α2-6-sialyltransferase cloned from Photobacterium damselae (Pd2,6ST) has been widely applied for the synthesis of various α2-6-linked sialosides. However, the extreme substrate flexibility of Pd2,6ST makes it unsuitable for site-specific α2-6-sialylation of complex substrates containing multiple galactose and/or N-acetylgalactosamine units. To tackle this problem, a general redox-controlled site-specific sialylation strategy using Pd2,6ST is described. This approach features site-specific enzymatic oxidation of galactose units to mask the unwanted sialylation sites and precisely controlling the site-specific α2-6-sialylation at intact galactose or N-acetylgalactosamine units.
从 Photobacterium damselae（Pd2,6ST）克隆的第一个细菌 α2-6-唾液酸转移酶已被广泛应用于各种 α2-6 连接唾液酸苷的合成。然而，Pd2,6ST 极端的底物灵活性使得它不适合于含有多个半乳糖和/或 N-乙酰半乳糖胺单元的复杂底物的特异性 α2-6-唾液酸化。为了解决这个问题，描述了一种使用 Pd2,6ST 的通用氧化还原控制的特异性唾液酸化策略。该方法的特点是特异性酶促氧化半乳糖单元，以掩盖不需要的唾液酸化位点，并精确控制完整的半乳糖或 N-乙酰半乳糖胺单元的特异性 α2-6-唾液酸化。
