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Biochemistry|June 24, 1998
The influence of the regulatory chain amino acids Glu-62 and IIe-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylaseM Dutta, E R KantrowitzThe Journal of Biological Chemistry|December 16, 1994
Mutations at histidine 412 alter zinc binding and eliminate transferase activity in Escherichia coli alkaline phosphataseL Ma, E R KantrowitzBiochemistry|December 26, 1989
Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylaseW Xu, E R KantrowitzBiochemistry|August 6, 1991
A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activityX Xu, E R KantrowitzBiochemistry|March 5, 1991
Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylaseW Xu, E R KantrowitzBiochemistry|February 20, 1996
Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sitesL Ma, E R KantrowitzProtein Engineering|November 1, 1989
Alteration of aspartate 101 in the active site of Escherichia coli alkaline phosphatase enhances the catalytic activityA Chaidaroglou, E R KantrowitzBiochemistry|October 12, 1993
Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanismX Xu, E R KantrowitzBiochemistry|January 28, 1992
Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesisY Zhang, E R KantrowitzBiochemical and Biophysical Research Communications|June 30, 1993
The Ala-161-->Thr substitution in Escherichia coli alkaline phosphatase does not result in loss of enzymatic activity although the homologous mutation in humans causes hypophosphatasiaA Chaidaroglou, E R KantrowitzPageof 22