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Helicobacter hepaticus Hh0072 gene encodes a novel α1-3-fucosyltransferase belonging to CAZy GT11 family
- Zhang, Lei, Lau, Kam, Cheng, Jiansong, Yu, Hai, Li, Yanhong, Sugiarto, Go, Huang, Shengshu, Ding, Li, Thon, Vireak, Wang, Peng G., Chen, Xi
- Glycobiology 2010 v.20 no.9 pp. 1077-1088
- Helicobacter hepaticus, amino acid sequences, antigens, catalysts, genes, glycosyltransferases, molecular cloning, oligosaccharides, polysaccharides, sequence homology
- 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.