Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity

@article{Dennis2006StructureAM,
  title={Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity},
  author={R. J. Dennis and E. Taylor and Matthew S. Macauley and K. Stubbs and J. Turkenburg and S. Hart and G. N. Black and D. Vocadlo and G. Davies},
  journal={Nature Structural &Molecular Biology},
  year={2006},
  volume={13},
  pages={365-371}
}
  • R. J. Dennis, E. Taylor, +6 authors G. Davies
  • Published 2006
  • Medicine, Biology
  • Nature Structural &Molecular Biology
  • O-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three… CONTINUE READING

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