A novel alpha-2,6-sialyltransferase: Transfer of sialic acid to fucosyl and sialyl trisaccharides

被引:52
作者
Kajihara, Y [1 ]
Yamamoto, T [1 ]
Nagae, H [1 ]
Nakashizuka, M [1 ]
Sakakibara, T [1 ]
Terada, I [1 ]
机构
[1] JAPAN TOBACCO INC,SEA WATER SCI RES LAB,ODAWARA,KANAGAWA 256,JAPAN
关键词
D O I
10.1021/jo961214v
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
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%).
引用
收藏
页码:8632 / 8635
页数:4
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