Staudacher E, März L
Institut für Chemie, Universität für Bodenkultur, Vienna, Austria.
Glycoconj J. 1998 Apr;15(4):355-60. doi: 10.1023/a:1006969701231.
In insect cells fucose can be either alpha1,6- or alpha1,3-linked to the asparagine-bound GlcNAc residue of N-glycans. Difucosylated glycans have also been found. Kinetic studies and acceptor competition experiments demonstrate that two different enzymes are responsible for this alpha1,6- and alpha1,3-linkage of fucose. Using dansylated acceptor substrates a strict order of these enzymes can be established for the formation of difucosylated structures. First, the alpha1,6-fucosyltransferase catalyses the transfer of fucose into alpha1,6-linkage to the non-fucosylated acceptor and then the alpha1,3-fucosyltransferase completes the difucosylation.
在昆虫细胞中，岩藻糖可以通过α1,6-或α1,3-连接到N-聚糖中与天冬酰胺结合的GlcNAc残基上。也发现了双岩藻糖化聚糖。动力学研究和受体竞争实验表明，两种不同的酶负责岩藻糖的这种α1,6-和α1,3-连接。使用丹磺酰化受体底物，可以确定这些酶形成双岩藻糖化结构的严格顺序。首先，α1,6-岩藻糖基转移酶催化岩藻糖转移到α1,6-连接的非岩藻糖化受体上，然后α1,3-岩藻糖基转移酶完成双岩藻糖化。
