Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion.

@article{Zalatan2008ComparativeEI,
  title={Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion.},
  author={Jesse G. Zalatan and Timothy David Fenn and Daniel Herschlag},
  journal={Journal of molecular biology},
  year={2008},
  volume={384 5},
  pages={1174-89}
}
Mechanistic models for biochemical systems are frequently proposed from structural data. Site-directed mutagenesis can be used to test the importance of proposed functional sites, but these data do not necessarily indicate how these sites contribute to function. In this study, we applied an alternative approach to the catalytic mechanism of alkaline phosphatase (AP), a widely studied prototypical bimetallo enzyme. A third metal ion site in AP has been suggested to provide general base catalysis… CONTINUE READING

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Comparative Enzymology in the AP

  • J. G. Zalatan, I. Catrina, R. Mitchell, P. K. Grzyska
  • J. Am. Chem
  • 2007
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