Specificities ofN-Acetylglucosamine-6-O-sulfotransferases in Relation to L-selectin Ligand Synthesis and Tumor-associated Enzyme Expression*

@article{Uchimura2002SpecificitiesOI,
  title={Specificities ofN-Acetylglucosamine-6-O-sulfotransferases in Relation to L-selectin Ligand Synthesis and Tumor-associated Enzyme Expression*},
  author={K. Uchimura and F. Elfasakhany and M. Hori and S. Hemmerich and Sarah E. Blink and G. Kansas and A. Kanamori and K. Kumamoto and R. Kannagi and T. Muramatsu},
  journal={The Journal of Biological Chemistry},
  year={2002},
  volume={277},
  pages={3979 - 3984}
}
  • K. Uchimura, F. Elfasakhany, +7 authors T. Muramatsu
  • Published 2002
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • N-Acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) catalyzes the transfer of sulfate from adenosine 3′-phosphate,5′-phosphosulfate to the C-6 position of the non-reducing GlcNAc. Three human GlcNAc6STs, namely GlcNAc6ST-1, GlcNAc6ST-2 (HEC-GlcNAc6ST), and GlcNAc6ST-3 (I-GlcNAc6ST), were produced as fusion proteins to protein A, and their substrate specificities as well as their enzymological properties were determined. Both GlcNAc6ST-1 and GlcNAc6ST-2 efficiently utilized the following… CONTINUE READING
    Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.
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