;Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
;
J.Mol.Biol. (1995)
Magnesium in the Active Site of Escherichia Coli Alkaline Phosphatase is Important for Both Structural Stabilization and Catalysis
Biochemistry (1993)
;Conversion of a Magnesium Binding Site Into a Zinc Binding Site by a Single Amino Acid Substitution in Escherichia Coli Alkaline Phosphatase
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J.Biol.Chem. (1993)
Reaction Mechanism of Alkaline Phosphatase Based on Crystal Structures. Two Metal Ion Catalysis
J.Mol.Biol. (1991)