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

Abstract

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 Lex, Ley, blood group H1-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 Ley-3FL and Ley-Lex-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.