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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, 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.