Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate

@article{Vocadlo2001CatalysisBH,
  title={Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate},
  author={David J. Vocadlo and G. Davies and R. Laine and Stephen G. Withers},
  journal={Nature},
  year={2001},
  volume={412},
  pages={835-838}
}
  • David J. Vocadlo, G. Davies, +1 author Stephen G. Withers
  • Published 2001
  • Chemistry, Medicine
  • Nature
  • Hen egg-white lysozyme (HEWL) was the first enzyme to have its three-dimensional structure determined by X-ray diffraction techniques. A catalytic mechanism, featuring a long-lived oxocarbenium-ion intermediate, was proposed on the basis of model-building studies. The ‘Phillips’ mechanism is widely held as the paradigm for the catalytic mechanism of β-glycosidases that cleave glycosidic linkages with net retention of configuration of the anomeric centre. Studies with other retaining… CONTINUE READING
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    References

    SHOWING 1-10 OF 41 REFERENCES
    Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site.
    • 78
    • PDF
    Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme.
    • 126
    • PDF