Abstract
Lewis x (Lex) and sialyl Lewis x (SLex)-containing glycans play important roles in numerous physiological and pathological processes. The key enzyme for the final step formation of these Lewis antigens is α1-3-fucosyltransferase. Here we report molecular cloning and functional expression of a novel Helicobacter hepaticus α1-3- fucosyltransferase (HhFT1) which shows activity towards both non-sialylated and sialylated Type II oligosaccharide acceptor substrates. It is a promising catalyst for enzymatic and chemoenzymatic synthesis of Lex, sialyl Lex and their derivatives. Unlike all other α1-3/4- fucosyltransferases characterized so far which belong to Carbohydrate Active Enzyme (CAZy, http://www.cazy.org/) glycosyltransferase family GT10, the HhFT1 shares protein sequence homology with α1-2-fucosyltransferases and belongs to CAZy glycosyltransferase family GT11. The HhFT1 is thus the first α1-3-fucosyltransferase identified in the GT11 family. © 2010 The Author.
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Zhang, L., Lau, K., Cheng, J., Yu, H., Li, Y., Sugiarto, G., … Chen, X. (2010). Helicobacter hepaticus Hh0072 gene encodes a novel α1-3- fucosyltransferase belonging to CAZy GT11 family. Glycobiology, 20(9), 1077–1088. https://doi.org/10.1093/glycob/cwq068
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