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Biochemistry|August 5, 2000
Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatasesK M Holtz, I E Catrina, A C Hengge, et al.The Journal of Biological Chemistry|November 22, 1996
Engineered complementation in Escherichia coli aspartate transcarbamoylase. Heterotropic regulation by quaternary structure stabilizationJ M Aucoin, E J Pishko, D P Baker, et al.Journal of Molecular Biology|August 25, 1983
Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutionsR S Silver, J P Daigneault, P D Teague, et al.Journal of Molecular Biology|May 23, 1998
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102B Stec, M J Hehir, C Brennan, et al.Biochemistry|January 12, 1988
Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylaseM M Ladjimi, S A Middleton, K S Kelleher, et al.Proceedings of the National Academy of Sciences of the United States of America|December 9, 1998
Yeast chorismate mutase in the R state: simulations of the active siteJ Ma, X Zheng, G Schnappauf, et al.Proceedings of the National Academy of Sciences of the United States of America|March 1, 1989
Molecular structure of fructose-1,6-bisphosphatase at 2.8-A resolutionH Ke, C M Thorpe, B A Seaton, et al.Biochemistry|February 16, 1993
Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysisC M Janeway, X Xu, J E Murphy, et al.Protein Science : a Publication of the Protein Society|February 1, 1995
Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylaseD P Baker, L Fetler, R T Keiser, et al.Journal of Molecular Biology|April 5, 1990
Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolutionH M Ke, C M Thorpe, B a Seaton, et al.Pageof 22