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利用链霉菌属的内切α-N-乙酰半乳糖胺酶通过转糖基化高效合成O-连接糖肽

Efficient synthesis of O-linked glycopeptide by a transglycosylation using endo alpha-N-acetylgalactosaminidase from Streptomyces sp.

作者信息

Ajisaka K, Miyasato M, Ishii-Karakasa I

机构信息

Nutrition Science Institute, Meiji Milk Products Co. Ltd., Odawara, Kanagawa, Japan.

出版信息

Biosci Biotechnol Biochem. 2001 May;65(5):1240-3. doi: 10.1271/bbb.65.1240.

DOI:10.1271/bbb.65.1240
PMID:11440149
Abstract

Gal beta-(1-->3)-GalNAc-linked hexapeptide was synthesized by a transglycosylation using Gal beta-(1-->3)-GalNAc beta-pNP as a donor and a serine-containing hexapeptide as an acceptor using endo GalNAc-ase from Streptomyces sp.. The Gal beta-(1-->3)-GalNAc residue was transferred to the hydroxyl group of the serine residue of the peptide. The total yield of the glycopeptide via this process was better than that of the chemoenzymatic method. This process was confirmed to be a versatile method for the synthesis of O-linked glycopeptides.

摘要

使用来自链霉菌属的N-乙酰半乳糖胺内切酶,以β-(1→3)-N-乙酰半乳糖胺β-对硝基苯酯为供体、含丝氨酸的六肽为受体,通过转糖基化反应合成了β-(1→3)-N-乙酰半乳糖胺连接的六肽。β-(1→3)-N-乙酰半乳糖胺残基转移到了肽的丝氨酸残基的羟基上。通过该过程得到的糖肽总产率优于化学酶法。该过程被证实是一种合成O-连接糖肽的通用方法。

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