牛初乳CMP-唾液酸：β-半乳糖（1→4）-N-乙酰葡糖胺-R α（2→6）-唾液酸转移酶参与了牛乳糖蛋白N-连接聚糖上末端唾液酸α（2→6）-N-乙酰半乳糖胺β（1→4）-N-乙酰葡糖胺序列的合成。
Bovine colostrum CMP-NeuAc:Gal beta(1-->4)GlcNAc-R alpha(2-->6)-sialyltransferase is involved in the synthesis of the terminal NeuAc alpha(2-->6)GalNAc beta(1-->4)GlcNAc sequence occurring on N-linked glycans of bovine milk glycoproteins.
作者信息
Nemansky M, Van den Eijnden D H
机构信息
Department of Medical Chemistry, Vrije Universiteit, Amsterdam, The Netherlands.
出版信息
Biochem J. 1992 Oct 1;287 ( Pt 1)(Pt 1):311-6. doi: 10.1042/bj2870311.
Abstract
Bovine colostrum CMP-NeuAc:Gal beta(-->4)GlcNAc-R alpha(2-->6)-sialyltransferase (alpha 6-sialyltransferase) appears to be capable of catalysing alpha 6-sialylation of the disaccharide GalNAc beta(1-->4)GlcNAc to yield the trisaccharide NeuAc alpha(2-->6)GalNAc beta(1-->4)GlcNAc. This provides an enzymic basis for the occurrence of this sialylated structure on the N-linked glycans of a number of bovine milk glycoproteins. Competition experiments using Gal beta(1-->4)GlcNAc and GalNAc beta(-->4)GlcNAc as acceptors indicate that both substrates are recognized by a single active site on the alpha 6-sialyltransferase. Extrapolation of these results suggests that the NeuAc alpha(2-->6)GalNAc beta(1-->4)GlcNAc structural element occurring on the N-linked glycans of several human glycoproteins are similarly synthesized by the action of a Gal beta(1-->4)GlcNAc-R alpha(2-->6)-sialyltransferase.
摘要
牛初乳CMP - 唾液酸：Galβ（→4）GlcNAc - Rα（2→6）-唾液酸转移酶（α6 - 唾液酸转移酶）似乎能够催化二糖GalNAcβ（1→4）GlcNAc的α6 - 唾液酸化反应，生成三糖NeuAcα（2→6）GalNAcβ（1→4）GlcNAc。这为多种牛乳糖蛋白N - 连接聚糖上这种唾液酸化结构的出现提供了酶学基础。使用Galβ（1→4）GlcNAc和GalNAcβ（→4）GlcNAc作为受体的竞争实验表明，这两种底物都被α6 - 唾液酸转移酶上的单个活性位点识别。这些结果的推断表明，几种人糖蛋白N - 连接聚糖上出现的NeuAcα（2→6）GalNAcβ（1→4）GlcNAc结构元件同样是由Galβ（1→4）GlcNAc - Rα（2→6）-唾液酸转移酶的作用合成的。
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