Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1.

@article{Kakuda2004StructuralBF,
  title={Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1.},
  author={Shinako Kakuda and Tetsuo Shiba and Masji Ishiguro and Hideki Tagawa and Shogo Oka and Yasuhiro Kajihara and Toshisuke Kawasaki and Soichi Wakatsuki and Ryuichi Kato},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 21},
  pages={
          22693-703
        }
}
The HNK-1 carbohydrate epitope is found on many neural cell adhesion molecules. Its structure is characterized by a terminal sulfated glucuronyl acid. The glucuronyltransferases, GlcAT-P and GlcAT-S, are involved in the biosynthesis of the HNK-1 epitope, GlcAT-P as the major enzyme. We overexpressed and purified the recombinant human GlcAT-P from Escherichia coli. Analysis of its enzymatic activity showed that it catalyzed the transfer reaction for N-acetyllactosamine (Galbeta1-4GlcNAc) but not… CONTINUE READING
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