Structure and mechanism of alkaline phosphatase.

  title={Structure and mechanism of alkaline phosphatase.},
  author={Joseph E. Coleman},
  journal={Annual review of biophysics and biomolecular structure},
  • J. Coleman
  • Published 1992
  • Chemistry, Medicine
  • 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… Expand
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Significant differences in dimeric structure stability of apo-enzymes were observed between EAP and BIAP, as well as in the kinetics of their activity and secondary structure recoveries, suggesting that distinct and subtle structural changes are required for their optimal activity recoveries. Expand
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D ow nl oa de d fro m a rjo ur na ls. an nu al re vi ew s.o rg by U ni ve rs ity o f W isc on sin Ea u Cl ai re (M cI nt yr
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Clinical Utilization of Alkaline Phosphatase Measurements