Pons, J., Stratton, J.R. and Kirsch, J.F.: How Do Two Unrelated Antibodies, Hyhel-10 and F9.13.7 Recognize the Same Epitope of Hen Egg-White Lysozyme? Protein Science, 11, 2308-2315 (2002). Medline Abstract Deu, E., Koch, K. A., and Kirsch, J. F.: The Role of the Conserved Intersubunit Salt Bridge, Lys68*:Glu265 in Aspartate Aminotransferase Kinetics. Multiple Forced Covariant Amino Acid Substitutions in Natural Variants. Protein Science, 11, 1062-1073 (2002).Medline Abstract Rajpal A., Kirsch, J. F.: Role of the minor energetic determinants of chicken egg white lysozyme(HEWL) to the stability of the HEWL.antibody scFv-10 complex. Proteins, 40, 49-57(2000). Medline Abstract Pons, J., Rajpal, A., and Kirsch, J. F.: Energetic analysis of an antigen/antibody interface: alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction. Protein Science, 8, 958-968 (1999). Medline Abstract Taylor, M. G., Rajpal, A. and Kirsch, J. F.: Kinetic Epitope Mapping of the Chicken Lysozyme HyHel-10 Fab Complex: Delineation of Docking Trajectories. Protein Science, 7, 1857-1867 (1998). Protein Science Abstract Rajpal, A, Taylor, M. G., and Kirsch, J. F.: Quantitative Evaluation of the Chicken Lysozyme Epitope in the HyHel-10 Fab Complex: Free Energies and Kinetics. Protein Science, 7, 1868-1874 (1998). Protein Science Abstract Kam-Morgan, L. N. W., Lavoie, T. B., Smith-Gill, S. J., and Kirsch, J. F.: Site-Directed Mutagenesis as a Tool in the Analysis of Protein-Protein Interactions. Methods in Enzymology 224, 503- 516 (1993). Medline Abstract Kam-Morgan, L N. W, Smith-Gill, S. J, Taylor, M.G., Zhang, L, Wilson, A. C., and Kirsch, J. F.: High Resolution Mapping of the HyHEL-10 Epitope of Hen Lysozyme by Site-Directed Mutagenesis. Proc. Natl. Acad. Sci. USA. 90, 3958-3962 (1993). Medline AbstractReturn to Research Page
Shaffer, W. A., Luong, T. N., Rothman, S. C. and Kirsch, J. F.: Quantitative Chimeric Analysis of Six Specificity Determinants that Differentiate E. coli Aspartate from Tyrosine Aminotransferase. Protein Science, 11, 2848-2859. (2002) Medline Abstract Eliot, A. E., Sandmark, J., Schneider, G., and Kirsch, J.F.: The Dual-Specific Active of 7,8-Diaminopelargonic-Acid Synthase and the Effect of the R391A Mutation. Biochemistry, 41, 12582-12589 (2002). Medline Abstract Luong, T. N., and Kirsch, J. F.: A general method for the quantitative analysis of functional chimeras: Applications from site-directed mutagenesis and macromolecular association. Protein Science, 10, 581-591 (2001). Medline Abstract Geck, M. K., and Kirsch, J. F.: A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Biochemistry, 38, 8032-8037 (1999). Medline Abstract Park Y., Luo J., Schultz P.G., and Kirsch J.F.: Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism. Biochemistry, 36, 10517-10525 (1997). Medline Abstract Gloss, L. M., Spencer, D. E. and Kirsch, J. F.: Cysteine-191 in Aspartate Aminotransferases Appears to be Conserved Due to the Lack of a Neutral Mutation Pathway to the Functional Equivalent, Alanine-191. Proteins: Structure, Function and Genetics, 24, 195-208 (1996). Medline Abstract Goldberg, J. M. and Kirsch, J. F.: The Reaction Catalyzed by Escherichia coli Aspartate Aminotransferase has Multiple Partially Rate-Determining Steps, While that Catalyzed by the Y225F Mutant is Dominated by Ketimine Hydrolysis. Biochemistry, 35, 5280-5291 (1996). Medline Abstract Onuffer, J. J. and Kirsch, J. F.: Redesign of the Substrate Specificity of Escherichia coli Aspartate Aminotransferase to that of Escherichia coli Tyrosine Aminotransferase by Homology Modeling and Site-directed Mutagenesis. Protein Science 4, 1750-1757 (1995). Medline Abstract Park Y., Luo J., Schultz P.G., Kirsch J.F.: Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism. Biochemistry 36, 10517-10525 (1997) Medline Abstract Gloss, L. M. and Kirsch, J. F.: Examining the Structural and Chemical Flexibility of the Active site Base, Lys-258, of Escherichia coli Aspartate Aminotransferase by Replacement with Unnatural Amino Acids. Biochemistry 34, 12323-12332 (1995). Medline Abstract Onuffer, J. J. and Kirsch, J. F.: Characterization of the Apparent Negative Cooperativity Induced in Escherichia coli Aspartate Aminotransferase by the Replacement of Aspartate 222 with Alanine. Evidence for an Extremely Slow Conformational Change. Protein Engineering 7, 413-424 (1994). Medline AbstractReturn to Research Page
Capitani, G., McCarthy, D. L., Gut, H., Grütter, M. G., and Kirsch, J. F.: Apple ACC Synthase in Complex with the Inhibitor L-aminoethoxyvinylglycine: Evidence for a Ketimine Intermediate. J. Biol. Chem., 277, 49735-49742 (2002). Medline Abstract Eliot, A. C., and Kirsch, J. F.: Modulation of the Internal Aldimine pKa's of of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues. Biochemistry, 41, 3836-3842 (2002). Medline Abstract McCarthy, D. L., Capitani, G., Feng, L., Gruetter, M. G. and Kirsch, J. F.: Glutamate 47 in 1-Aminocyclopropane-1-carboxylate Synthase is a Major Specificity Determinant. Biochemistry, 40, 12276-12284 (2001). Medline Abstract Koch, K.A., Capitani, G., Grueter, M. G., and Kirsch, J. F.: The Human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-carboxylate sythase encodes a protein lacking that activity. Gene, 272, 75-84 (2001). Medline Abstract Feng, L., Geck, M. K., Eliot, A. C., and Kirsch, J. F.: Aminotransferase Activity and Bioinformatic Analysis of 1-Aminocyclopropane-1-carboxylate Synthase. Biochemistry (2000). Medline Abstract Feng L., Kirsch, J. F.: L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry, 39, 2436-44 (2000). Medline Abstract Capitani, G., Hohenester, E., Feng, L., Storici, P., Kirsch, J. F., and Jansonius, J. N.: Structure of 1-Aminocyclopropane-1-carboxylate Synthase, a Key Enzyme in the Biosynthesis of the Plant Hormone Ethylene. Journal of Molecular Biology, 294, 743-756 (1999). Medline Abstract Li Y., Feng L., and Kirsch, J.F.: Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase. Biochemistry, 36, 15477-15488 (1997). Medline Abstract White, M. F., Vasquez, J., Yang, S-F., and Kirsch, J. F.: Expression of Apple 1-aminocyclopropane-1-carboxylate Synthase in E. coli: Kinetic Characterization of Wild-type and Active-site Mutant Forms. Proc. Natl. Acad. Sci USA. 91, 12428-12432 (1994). Medline Abstract Hohenester, E., White, M. F., Kirsch, J. F., and Jansonius, J. N.: Crystallization and Preliminary X-ray Analysis of Recombinant 1- Aminocyclopropane-1-carboxylate Synthase from Apple, a Key Enzyme in the Biosynthesis of the Plant Hormone Ethylene. J. Mol. Biol. 243, 947-949 (1994). Medline AbstractReturn to Research Page
Shih, P., and Kirsch, J. F.: Design and Structural Analysis of an Engineered Thermostable Chicken Lysozyme. Protein Science, 14, 2063-2072 (1995). Medline Abstract Shih, P., Holland, D. R. and Kirsch, J. F.: Thermal Stability Determinants of Chicken Egg-White Lysozyme Core Mutants: Hydrophobicity, Packing Volume, and Conserved Buried Water Molecules. Protein Science, 14, 2052-2062 (1995). Medline Abstract Matsumura, I and Kirsch, J. F.: Is Aspartate 52 Essential for Catalysis by Chicken Egg White Lysozyme? The Role of Natural Substrate-Assisted Hydrolysis. Biochemistry, 35, 1881-1890 (1996). Medline Abstract Matsumura, I and Kirsch, J. F.: Synergistic Contributions of Asparagine 46 and Aspartate 52 to the Catalytic Mechanism of Chicken Egg White Lysozyme. Biochemistry, 35, 1890-1896 (1996). Medline Abstract
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Departments of Molecular and Cell Biology and Chemistry University of California, Berkeley and Materials Sciences Division Lawrence Berkeley National Laboratory Berkeley, California 94720 +1-510-642-6368 jfkirsch@uclink4.berkeley.edu ![]() |
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