Kirsch Lab Selected Publications



Protein-Protein Interactions


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 Abstract


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Aminotransferase Mutagenesis

   
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 Abstract

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ACC Synthase


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 Abstract


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Lysozyme mechanism, thermostability, and evolution


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
copyright 1996 University of California
page maintained by Steve Rothman
created by Alan D. Miller