Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase.

@article{Murphy1993ConversionOA,
  title={Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase.},
  author={Jennifer E. Murphy and Xiao Qin Xu and Evan R. Kantrowitz},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 29},
  pages={21497-500}
}
The replacement of aspartic acid by histidine at position 153 in Escherichia coli alkaline phosphatase results in a mutant enzyme that is remarkably similar to certain mammalian alkaline phosphatases that are activated by magnesium in a time-dependent fashion. These mammalian alkaline phosphatases have histidine at the position corresponding to 153 of the E. coli sequence. Here we report the three-dimensional structure of the mutant E. coli alkaline phosphatase with histidine at position 153… CONTINUE READING