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.
Original language | English (US) |
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Pages (from-to) | 1077-1088 |
Number of pages | 12 |
Journal | Glycobiology |
Volume | 20 |
Issue number | 9 |
DOIs | |
State | Published - Sep 2010 |
Keywords
- cloning
- fucosyltransferase
- Helicobacter hepaticus
- Lewis x
- sialyl Lewis x
ASJC Scopus subject areas
- Biochemistry