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糖基转移酶的底物和供体特异性。

Substrate and donor specificity of glycosyl transferases.

作者信息

Ernst B, Oehrlein R

机构信息

University of Basel, Institute of Molecular Pharmacy, Switzerland.

出版信息

Glycoconj J. 1999 Feb;16(2):161-70. doi: 10.1023/a:1026496714403.

Abstract

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.

摘要

已表明所有选择素均识别碳水化合物表位唾液酸化路易斯(x)和唾液酸化路易斯(a)。因此,为了建立构效关系,高效合成这些四糖及其衍生物至关重要。本文总结了糖基转移酶介导的方法,重点介绍了修饰受体和修饰糖核苷酸供体的使用。对所涉及的酶:β(1-3)和β(1-4)半乳糖基转移酶、α(2-3)唾液酸转移酶、FucT III和FucT VI的研究表明,酶促合成对于快速制备唾液酸化路易斯(x)和唾液酸化路易斯(a)衍生物非常高效。

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