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Journal of Molecular Biology|April 5, 1996
Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphataseT T Tibbitts, J E Murphy, E R Kantrowitz
Biotechnology and Bioengineering|April 1, 1979
Process characteristics of cell lysis mutants of Saccharomyces cerevisiaeJ Boudrant, J DeAngelo, A J Sinskey, et al.
Biochemical and Biophysical Research Communications|February 27, 1996
Glutamic acid residue 98 is critical for catalysis in pig kidney fructose-1,6-bisphosphataseN Kelley, E L Giroux, G Lu, et al.
Nature Structural Biology|August 1, 1997
Trapping and visualization of a covalent enzyme-phosphate intermediateJ E Murphy, B Stec, L Ma, et al.
Protein Science : a Publication of the Protein Society|November 1, 1996
The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closureD P Baker, L Fetler, P Vachette, et al.
Protein Science : a Publication of the Protein Society|November 1, 1996
Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativityG Lu, B Stec, E L Giroux, et al.
Protein Science : a Publication of the Protein Society|May 25, 1999
Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stabilityD C Martin, S C Pastra-Landis, E R Kantrowitz
Protein Science : a Publication of the Protein Society|November 1, 1994
Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structureP Tauc, R T Keiser, E R Kantrowitz, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 29, 1999
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidaseN Sträter, L Sun, E R Kantrowitz, et al.
Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.
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