• Medicine, Chemistry
• Published in Nature 2001
• DOI:10.1038/35090602

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 Gideon J. Davies and Roger A. Laine and Stephen G. Withers},
  journal={Nature},
  year={2001},
  volume={412},
  pages={835-838}
}

• David J. Vocadlo, Gideon J. Davies, +1 author Stephen G. Withers

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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