Human N-acetylglucosaminyltransferase I. Expression in Escherichia coli as a soluble enzyme, and application as an immobilized enzyme for the chemoenzymatic synthesis of N-linked oligosaccharides.

@article{Fujiyama2001HumanNI,
  title={Human N-acetylglucosaminyltransferase I. Expression in Escherichia coli as a soluble enzyme, and application as an immobilized enzyme for the chemoenzymatic synthesis of N-linked oligosaccharides.},
  author={Kazuhito Fujiyama and Yoshihiro Ido and Ryo Misaki and Daniel G. Moran and Itaru Yanagihara and Toshiyuki Honda and Shuhei Nishimura and Tadashi Yoshida and Takahiro Seki},
  journal={Journal of bioscience and bioengineering},
  year={2001},
  volume={92 6},
  pages={
          569-74
        }
}
N-Acetylglucosaminyltransferase I (GnT-I), which catalyzes the transfer of an N-acetylglucosamine residue from UDP-N-acetylglucosamine to the alpha1,3-linked mannose on Man5GlcNAc2 (M5), is a critical enzyme for the synthesis of high-mannose-type to complex-type glycan structures in N-linked glycan processing. We developed a large-scale preparation system for recombinant human GnT-I (hGnT-I) using the maltose binding protein (MBP) fusion system to facilitate the chemoenzymatic route for complex… CONTINUE READING