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Substrate Characterization of Bacteroides fragilis α1,3/4-Fucosyltransferase Enabling Access to Programmable One-Pot Enzymatic Synthesis of KH-1 Antigen
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Substrate Characterization of Bacteroides fragilis α1,3/4-Fucosyltransferase Enabling Access to Programmable One-Pot Enzymatic Synthesis of KH-1 Antigen

Hsin-Hui Huang, Jia-Lin Fang, Hung-Kai Wang, Chih-Yuan Sun, Teng-Wei Tsai, Yu-Ting Huang, Cheng-Yu Kuo, Yi-Jyun Wang, Chi-Chun Liao 和 Ching-Ching Yu
ACS Catalysis, 卷.9(12), 頁碼.11794-11800
12/2019
DOI: https://doi.org/10.1021/acscatal.9b04182

摘要

enzymatic synthesis fucosyltransferase human milk oligosaccharides KH-1 antigen tumor-associated carbohydrate antigen Catalysis Chemistry (all)
Bacteroides fragilis α1,3/4-fucosyltransferase (Bf13FT) was expressed in Escherichia coli and characterized as an α1,3/4-fucosyltransferase that can be used as a versatile catalyst for the synthesis of various fucosides, including Le x , Le y , blood group H 1 -antigen, 3FL, LNFP III, LNFP V, LNnFP V, LNDFH II, LNDFH III, IFLNH III, DF-pLNnH, and TF-pLNnH, and hybrid-type glycans, such as Le y -3FL and Le y -Le x -3FL. The preferential fucosylation activity on Fucα1,2LacNAc and LacNAc over Lac, which enabled programmable fucosylation, led to the one-pot synthesis of a KH-1 antigen.

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