Comparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active-Site Metal Ion

This publication has 68 references indexed in Scilit:

• Promiscuous Sulfatase Activity and Thio-Effects in a Phosphodiesterase of the Alkaline Phosphatase Superfamily
  Biochemistry, 2008
• Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase
  Biochemistry, 2008
• Structure and Molecular Mechanism of Bacillus anthracis Cofactor-Independent Phosphoglycerate Mutase: A Crucial Enzyme for Spores and Growing Cells of Bacillus Species
  Biophysical Journal, 2007
• Type II restriction endonucleases: structure and mechanism
  Cellular and Molecular Life Sciences, 2005
• Coot: model-building tools for molecular graphics
  Acta Crystallographica Section D Structural Biology, 2004
• Artificial Evolution of an Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia coli Alkaline Phosphatase
  Journal of Molecular Biology, 2002
• A revised mechanism for the alkaline phosphatase reaction involving three metal ions
  Journal of Molecular Biology, 2000
• [20] Processing of X-ray diffraction data collected in oscillation mode
  1997
• Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
  Nature, 1992
• Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin
  Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences, 1986