Structure and mechanism of alkaline phosphatase.

@article{Coleman1992StructureAM,
  title={Structure and mechanism of alkaline phosphatase.},
  author={J. Coleman},
  journal={Annual review of biophysics and biomolecular structure},
  year={1992},
  volume={21},
  pages={
          441-83
        }
}
  • J. Coleman
  • Published 1992
  • Medicine, Chemistry
  • Annual review of biophysics and biomolecular structure
  • Alkaline phosphatase was the first zinc enzyme to be discovered in which three closely spaced metal ions (two Zn ions and one Mg ion) are present at the active center. Zn ions at all three sites also produce a maximally active enzyme. These metal ions have center-to-center distances of 3.9 A (Zn1-Zn2), 4.9 A (Zn2-Mg3), and 7.1 A (Zn1-Mg3). Despite the close packing of these metal centers, only one bridging ligand, the carboxyl of Asp51, bridges Zn2 and Mg3. A crystal structure at 2.0-A… CONTINUE READING
    X-Ray Structure Reveals a New Class and Provides Insight into Evolution of Alkaline Phosphatases
    15
    Cocatalytic Zinc Sites
    2

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