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Protein Science : a Publication of the Protein Society|August 1, 1995
Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sitesL Ma, T T Tibbitts, E R Kantrowitz
The Journal of Biological Chemistry|June 10, 1980
The role of tryptophan in aspartate transcarbamylaseJ Foote, D M Ikeda, E R Kantrowitz
Journal of Molecular Biology|June 30, 2000
A revised mechanism for the alkaline phosphatase reaction involving three metal ionsB Stec, K M Holtz, E R Kantrowitz
Protein Science : a Publication of the Protein Society|March 30, 2000
The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylaseJ B Sakash, A Tsen, E R Kantrowitz
The Journal of Biological Chemistry|December 16, 1994
Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibitionE Giroux, M K Williams, E R Kantrowitz
The Journal of Biological Chemistry|October 15, 1993
Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphataseJ E Murphy, X Xu, E R Kantrowitz
Biochimica Et Biophysica Acta|March 29, 1985
Affinity and hydrophobic chromatography of Escherichia coli aspartate transcarbamoylaseT P West, I Maldonado, E R Kantrowitz
The Journal of Biological Chemistry|March 20, 1999
A model of the transition state in the alkaline phosphatase reactionK M Holtz, B Stec, E R Kantrowitz
European Journal of Biochemistry|April 1, 1997
Room temperature phosphorescence study of phosphate binding in Escherichia coli alkaline phosphataseL Sun, E R Kantrowitz, W C Galley
Protein Science : a Publication of the Protein Society|November 1, 1994
Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active siteT T Tibbitts, X Xu, E R Kantrowitz
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