A novel alpha-2,6-sialyltransferase: Transfer of sialic acid to fucosyl and sialyl trisaccharides
A novel alpha-2,6-sialyltransferase: Transfer of sialic acid to fucosyl and sialyl trisaccharides
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DOI：
10.1021/jo961214v
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发表时间：
1996-11-29
影响因子：
3.6
通讯作者：
Terada, I
中科院分区：
文献类型：
--
作者：
Kajihara, Y;Yamamoto, T;Terada, I
对细菌α-2，6-唾液酸基转移酶的底物专一性和酶促唾液酸化能力进行了检测。酶活性测定表明，在末端半乳糖苷的2或3位有唾液酸基转移到含有岩藻糖苷或唾液糖苷的II型寡糖上的能力很强。酶法合成以Neu5Acβ2，3Galβ1，4Glc和Fucα1，2Galβ1，4Glc为唾液酸受体时发现的异常分析产物的结构。两个唾液酸化反应(10MU摩尔级)均用83M单位的酶，在2 h内完成，得到唾液酸苷类似物Neu5Acα2，6(Fucα1，2)Galβ1，4Glc(88%)和Neu5Ac Alpha 2，6(Neu5Ac beta 2，3)GalBeta 1，4Glc(92%)。
The substrate specificity and enzymatic sialylation ability of the bacterium alpha-2,6-sialyltransferase were examined. The enzyme assay displayed a remarkable ability to catalyze sialyl transfer to type-II oligosaccharides possessing fucoside or sialoside at the 2 or 3 position of the terminal galactoside. Enzymatic syntheses were performed in order to confirm the structure of unusual assay products found when using Neu5Ac beta 2,3Gal beta 1,4Glc and Fuc alpha 1,2Gal beta 1,4Glc as the sialyl accepters. Both sialylation reactions (10 mu mol scales) were run using 83 munits of enzyme, were complete in 2 h, and afforded the sialoside analogues Neu5Ac alpha 2,6(Fuc alpha 1,2) Gal beta 1,4Glc (88%) and Neu5Ac alpha 2,6(Neu5Ac beta 2,3) Gal beta 1,4Glc (92%).