William N. Lipscomb

Recent research of the Lipscomb group has been on zinc enzymes (leucine aminopeptidase) and on allosteric enzymes (chorismate mutase, fructose1,6-bisphosphatase and aspartate transcarbomylase. The emphasis is on active site mechanisms, and on transmission of conformational information from the allosteric site to the active site in the multi-subunit allosteric enzymes. Methods include single crystal X-ray diffraction, structures of mutants, and molecular dynamics.

Selected Publications

1. Lei Jin, Boguslaw Stec, William N. Lipscomb, and Evan R. Kantrowitz, 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 Å, Proteins: Structure, Function, and Genetics 37, 729-742 (1999).

2. Norbert Sträter, Lee Sun, E.R. Kantrowitz, and William N. Lipscomb, A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase, Proc. Natl. Acad. Sci. USA 96, 11151-11155 (1999).

3. Jianpeng Ma, Xiaofeng Zheng, Georg Schnappauf, Gerhard Braus, Martin Karplus and William N. Lipscomb, Yeast chorismate mutase in the R state: Simulations of the active site, Proc. Natl. Acad. Sci. USA 95, 14640-14645 (1998).

4. Norbert Sträter, Georg Schnappauf, Gerhard Braus and William N. Lipscomb, Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures, Structure 5, No. 11, 1438-1452 (1997).