Site-specific Fucosylation of Sialylated Polylactosamines by α1,3/4-Fucosyltransferases-V and -VI Is Defined by Amino Acids Near the N Terminus of the Catalytic Domain*

@article{Shetterly2007SitespecificFO,
  title={Site-specific Fucosylation of Sialylated Polylactosamines by $\alpha$1,3/4-Fucosyltransferases-V and -VI Is Defined by Amino Acids Near the N Terminus of the Catalytic Domain*},
  author={Susan Shetterly and Franziska Jost and Susan R. Watson and Ronald M. A. Knegtel and Bruce Macher and Eric H. Holmes},
  journal={Journal of Biological Chemistry},
  year={2007},
  volume={282},
  pages={24882 - 24892}
}
Fucose transfer from GDP-fucose to GlcNAc residues of the sialylated polylactosamine acceptor NeuAcα2-3Galβ1-4Glc-NAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1-4Glcβ1-ceramide leads to two isomeric monofucosyl antigens, VIM2 and sialyl-Lex. Human α1,3/4-fucosyltransferase (FucT)-V catalyzes primarily the synthesis of VIM2, whereas human FucT-VI catalyzes primarily the synthesis of sialyl-Lex. Thus, these two enzymes have distinct “site-specific fucosylation” properties. Amino acid sequence alignment of these… 
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