Selected Publications Haloalkanoate Dehalogenase Superfamily The X-ray Crystal Structure of the Hypothetical Phosphotyrosine Phosphatase MDP-1 of the HAD Superfamily Peisach, E., Selengut, J., Dunaway-Mariano, D., and Allen, K.N. Biochem. (2004). 43: 12770-9. Structural Origin of the High Affinity of a Chemically Evolved Lanthanide-Binding Peptide Nitz, M., Sherawat, M., Franz, K. J., Peisach, E., Allen, K. N., and Imperiali, B. Angew. Chemie. (2004). 28: 2037-45. Investigation of Metal Ion Binding in Phosphonoacetaldehyde Hydrolase Identifies Sequence Markers for Metal-Activated Enzymes of the HAD Enzyme Superfamily. Zhang, G, Morais, M.C., Dai, J., Zhang, W., Dunaway-Mariano, D., Allen, K.N. Biochem. (2004). 43: 2812-20. Analysis of the substrate specificity loop of the HAD superfamily cap domain. Lahiri, S.D., Zhang, G., Dai, J., Dunaway-Mariano, D., Allen, K.N. Biochem. (2004). 43: 4990-7. X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis. Morais, M. C., G. Zhang, W. Zhang, D. B. Olsen, D. Dunaway-Mariano and K. N. Allen J. Biol. Chem. (2004). 279(10): 9353-61. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Lahiri, S. D., G. Zhang, D. Dunaway-Mariano and K. N. Allen Science (2003). 299(5615): 2067-71. Enzymatic synthesis of radiolabeled phosphonoacetaldehyde. Zhang, G., K. N. Allen and D. Dunaway-Mariano. Anal Biochem (2003). 322(2): 233-7. Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis. Lahiri, S. D., G. Zhang, D. Dunaway-Mariano and K. N. Allen. Biochemistry (2002). 41(26): 8351-9. Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis. Zhang, G., A. S. Mazurkie, D. Dunaway-Mariano and K. N. Allen Biochemistry (2002). 41(45): 13370-7. Crystallization and preliminary X-ray diffraction studies of beta-phosphoglucomutase from Lactococcus lactus. Lahiri, S. D., G. Zhang, P. Radstrom, D. Dunaway-Mariano and K. N. Allen. Acta Cryst D Biol Crystallogr (2002). 58(Pt 2): 324-6. The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Morais, M. C., W. Zhang, A. S. Baker, G. Zhang, D. Dunaway-Mariano and K. N. Allen. Biochemistry (2000). 39(34): 10385-96. Crystallization and preliminary crystallographic analysis of phosphonoacetaldehyde hydrolase. Morais, M. C., A. S. Baker, D. Dunaway-Mariano and K. N. Allen. Acta Cryst D Biol Crystallogr (2000). 56 (Pt 2): 206-9.   Aldolase Isozymes Spatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose-1,6-bisphosphate aldolase. Pezza, J. A., K. H. Choi, T. Z. Berardini, P. T. Beernink, K. N. Allen and D. R. Tolan J. Biol. Chem. (2003). 278(19): 17307-13. Chemical-modification rescue assessed by mass spectrometry demonstrates that gamma-thia-lysine yields the same activity as lysine in aldolase. Hopkins, C. E., P. B. O'Connor, K. N. Allen, C. E. Costello and D. R. Tolan Protein Science (2002). 11(7): 1591-9. Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate. Choi, K. H., J. Shi, C. E. Hopkins, D. R. Tolan and K. N. Allen. Biochemistry (2001). 40(46): 13868-75. Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3A. Choi, K. H., A. S. Mazurkie, A. J. Morris, D. Utheza, D. R. Tolan and K. N. Allen. Biochemistry (1999). 38(39): 12655-64.   Miscellaneous X-Ray Structure Analysis of a Designed Oligomeric Mini-Protein Reveals a Discrete Quaternary Architecture Ali, M., Peisach, E., Allen, K.N., and Imperiali, B. Proc. Nat. Acad. Sci. (2004). 101: 12183-8. Phosphoryl Group Transfer: Evolution of a Catalytic Scaffold Allen, K.N. and Dunaway-Mariano, D. Trends. Biochem. Sci. (2004). 29: 495-503. The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex. Lahiri, S. D., P. F. Wang, P. C. Babbitt, M. J. McLeish, G. L. Kenyon and K. N. Allen. Biochemistry (2002). 41(47): 13861-7. The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale. Choi, K. H., R. A. Laursen and K. N. Allen. Biochemistry (1999). 38(36): 11624-33.