Home Faculty and Research Faculty by Name Jack Kirsch

Jack Kirsch

Professor of the Graduate School Division of Biochemistry and Molecular Biology

Lab Homepage: http://mcb.berkeley.edu/labs/kirsch/

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Research Interests

PLEASE NOTE.  PROFESSOR KIRSCH IS RETIRED AND IS NO LONGER ACCEPTING NEW STUDENTS OR POSTDOCTORAL FELLOWS.

We are currently engaged in collaborative research with Professors Steven Brenner and Michael Eisen.  The former effort is focused on developing improved methods for annotation of protein function from sequence and structural data, while the latter deals with determining the correlates of promotor site affinity with biological fitness.

Current Projects

In additon to the projects listed above, we maintain an active interest in mechanistic enzymology, especially pyridoxal phosphate dependent enzymes.  Other interests include protein/protein and protein/ small molecule interactions, as well as quantitative analysis of drug/target interactions.

Selected Publications

Computational Redesign of the SHV-1 ß-lactamase/ß-lactamase Inhibitor Protein Interface [K. A. Reynolds, M. S. Hanes, J. M. Thomson, A. J. Antczak, J. M. Berger, R. A. Bonomo, J. F. Kirsch, T. M.  Handel (2008)  J. Molec. Biol. 382, 1265-1275]

Identification of Mutations that Shift Paralog Functions: Conversion of E. Coli Malate Dehydrogenase to a Lactate Dehydrogenase by Rational Design [Y. Yin  and J. F. Kirsch (2007) Proceedings of the National Academy of Sciences, USA 104, 17353-17357]

The Unfolding Pathway for Apo E. coli Aspartate Aminotransferase is Dependent on the Choice of Denaturant [E. Deu, and J. F. Kirsch (2007) Biochemistry 46, 5810-5818]

The Narrow Substrate Specificity of Human Tyrosineaminotransferase - The Enzyme Deficient in Tyrosinemia Type II [ S. Sivaraman and J. F.  Kirsch (2006) FEBS Journal 273, 1920-1929]

Free Energies of Protein-Protein Association Determined by Electrospray Ionization Mass Spectrometry Correlate Accurately with Values Obtained by Solution Methods. [S. R. Krishnaswamy, E. R. Williams, and J. F.  Kirsch (2006) Protein Science 15,1465-1475]

The Enzymology of Cystathionine Biosynthesis: Strategies for the Control of Substrate and Reaction Specificity. [S. M. Aitken and J. F.  Kirsch (2005) Arch. Biochem. Biophys. 433, 166-175]

Directed Evolution Relieves Product Inhibition in a Rationally Designed Tyrosine Aminotransferase. [S. C. Rothman, M. Voorhies, and J. F. Kirsch (2004) Protein Science 13, 763-772]

Avoiding the Road Less Traveled: How the Topology of Enzyme-substrate Complexes Can Dictate Product Selection. [A. C. Eliot and J. F. Kirsch (2003) Accts. Chem. Res. 36, 757-765]

Pyridoxal Phosphate Enzymes: Mechanistic, Structural and Evolutionary Considerations. [A. C. Eliot, and J. F. Kirsch (2004) Ann. Revs. Biochem. 73, 383-415]

How Does an Enzyme Evolved in vitro Compare to Naturally Occurring Homologs Possessing the Targeted Function? Tyrosine Aminotransferase from Aspartate Aminotransferase. [S. C. Rothman and J. F. Kirsch (2003) J. Mol. Biol. 327 593-608]

Last Updated 2009-06-22