| Literature DB >> 20466652 |
Lei Zhang1, Kam Lau, Jiansong Cheng, Hai Yu, Yanhong Li, Go Sugiarto, Shengshu Huang, Li Ding, Vireak Thon, Peng G Wang, Xi Chen.
Abstract
Lewis x (Le(x)) and sialyl Lewis x (SLe(x))-containing glycans play important roles in numerous physiological and pathological processes. The key enzyme for the final step formation of these Lewis antigens is alpha1-3-fucosyltransferase. Here we report molecular cloning and functional expression of a novel Helicobacter hepaticus alpha1-3-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 Le(x), sialyl Le(x) and their derivatives. Unlike all other alpha1-3/4-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 alpha1-2-fucosyltransferases and belongs to CAZy glycosyltransferase family GT11. The HhFT1 is thus the first alpha1-3-fucosyltransferase identified in the GT11 family.Entities:
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Year: 2010 PMID: 20466652 PMCID: PMC2948817 DOI: 10.1093/glycob/cwq068
Source DB: PubMed Journal: Glycobiology ISSN: 0959-6658 Impact factor: 4.313