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Biochemistry|August 20, 1991
Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallographyH Kim, W N LipscombProceedings of the National Academy of Sciences of the United States of America|November 7, 1995
Location of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanismsY Xue, W N LipscombBiochemistry|November 14, 1995
Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallographyN Sträter, W N LipscombBiochemistry|December 12, 1989
Binding of sulfonamide and acetamide to the active-site Zn2+ in carbonic anhydrase: a theoretical studyJ Liang, W N LipscombBiochemistry|June 12, 1990
Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexesH Kim, W N LipscombBiochemistry|July 18, 1995
Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal formN Sträter, W N LipscombThe Journal of Biological Chemistry|November 25, 1991
The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sitesY Zhang, E R KantrowitzThe Journal of Biological Chemistry|August 15, 1992
The importance of aspartate 327 for catalysis and zinc binding in Escherichia coli alkaline phosphataseX Xu, E R KantrowitzBiochemistry|September 5, 1989
Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATPY Zhang, E R KantrowitzPageof 22