Substrate and donor specificity of glycosyl transferases

被引：28

作者：

Ernst, B

Oehrlein, R

机构：

[1] Univ Basel, Inst Mol Pharm, CH-4057 Basel, Switzerland

[2] Novartis Pharma AG, Dept Transplantat, CH-4002 Basel, Switzerland

来源：

GLYCOCONJUGATE JOURNAL | 1999年 / 16卷 / 02期

关键词：

sialyl Lewis(x); sialyl Lewis(a); enzymatic synthesis; substrate specificity; donor specificity; beta(1-3) galactosyl transferases; beta(1-4)galactosyl transferases; alpha(2-3)sialyl transferase; FucT III; FucT IV;

D O I：

10.1023/A:1026496714403

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It has been shown that all selectins recognize the carbohydrate epitopes sialyl Lewis(x) and sialyl Lewis(a). For the establishment of the structure-activity relationship, the efficient synthesis of these tetrasaccharides and derivatives is therefore of vital interest. The glycosyl transferase-mediated approach is summarized with emphasis on the use of modified acceptors and modified sugar-nucleotide donors. A survey of the involved enzymes: beta(1-3) and beta(1-4)galactosyl transferases, alpha(2-3)sialyl transferase, FucT III and FucT VI reveals that the enzymatic synthesis is highly efficient for the rapid preparation of sialyl Lewis(x)- and sialyl Lewis(a)-derivatives.

引用

页码：161 / 170

页数：10

共 74 条

[1]

[Anonymous], PHYSL PATHOPHYSIOLOG

[2]

ATS SC, 1994, CARBOHYD RES, V252, P325

[3] On the preparative use of recombinant β(1-3)galactosyl-transferase [J].