A structural view of the action of Escherichia coli (lacZ) beta-galactosidase.

@article{Juers2001ASV,
  title={A structural view of the action of Escherichia coli (lacZ) beta-galactosidase.},
  author={Douglas H Juers and Tom D Heightman and Andrea Vasella and John D. McCarter and Lloyd F Mackenzie and Stephen G Withers and Brian W. Matthews},
  journal={Biochemistry},
  year={2001},
  volume={40 49},
  pages={14781-94}
}
The structures of a series of complexes designed to mimic intermediates along the reaction coordinate for beta-galactosidase are presented. These complexes clarify and enhance previous proposals regarding the catalytic mechanism. The nucleophile, Glu537, is seen to covalently bind to the galactosyl moiety. Of the two potential acids, Mg(2+) and Glu461, the latter is in better position to directly assist in leaving group departure, suggesting that the metal ion acts in a secondary role. A sodium… CONTINUE READING

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