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Jack Kirsch

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Co-Publications
Name
9
Eliot, Andrew
6
Jansonius, Johan
6
Capitani, Guido
5
Gloss, Lisa
4
Aitken, Susan
4
Deu, Edgar
4
Rajpal, Arvind
3
Rothman, Steven
3
Luong, Tinh
3
Grütter, Markus
3
Christen, Philipp
3
Berger, James
3
Feng, L
2
Pons, Jaume
2
White, Malcolm

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Publications

TOP 3
Deu Edgar; Dhoot Jashdeep; Kirsch Jack F
The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure.
Reynolds Kimberly A; Hanes Melinda S; Thomson Jodi M; Antczak Andrew J; Berger James M; Bonomo Robert A; Kirsch Jack F; Handel Tracy M
Computational redesign of the SHV-1 beta-lactamase/beta-lactamase inhibitor protein interface.
Ma Enbo; MacRae Ian J; Kirsch Jack F; Doudna Jennifer A
Autoinhibition of human dicer by its internal helicase domain.

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All Publications

2009: Deu Edgar; Dhoot Jashdeep; Kirsch Jack F
The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure.
Biochemistry 2009;48(2):433-41.
2008: Reynolds Kimberly A; Hanes Melinda S; Thomson Jodi M; Antczak Andrew J; Berger James M; Bonomo Robert A; Kirsch Jack F; Handel Tracy M
Computational redesign of the SHV-1 beta-lactamase/beta-lactamase inhibitor protein interface.
Journal of molecular biology 2008;382(5):1265-75.
2008: Ma Enbo; MacRae Ian J; Kirsch Jack F; Doudna Jennifer A
Autoinhibition of human dicer by its internal helicase domain.
Journal of molecular biology 2008;380(1):237-43.
2008: Muratore Kathryn E; Srouji John R; Chow Margaret A; Kirsch Jack F
Recombinant expression of twelve evolutionarily diverse subfamily Ialpha aminotransferases.
Protein expression and purification 2008;57(1):34-44.
2007: Yin Yifeng; Kirsch Jack F
Identification of functional paralog shift mutations: conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase.
Proceedings of the National Academy of Sciences of the United States of America 2007;104(44):17353-7.
2007: Deu Edgar; Kirsch Jack F
Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme.
Biochemistry 2007;46(19):5819-29.
2007: Deu Edgar; Kirsch Jack F
The unfolding pathway for Apo Escherichia coli aspartate aminotransferase is dependent on the choice of denaturant.
Biochemistry 2007;46(19):5810-8.
2006: Reynolds Kimberly A; Thomson Jodi M; Corbett Kevin D; Bethel Christopher R; Berger James M; Kirsch Jack F; Bonomo Robert A; Handel Tracy M
Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface.
The Journal of biological chemistry 2006;281(36):26745-53.
2006: Krishnaswamy Sanjay R; Williams Evan R; Kirsch Jack F
Free energies of protein-protein association determined by electrospray ionization mass spectrometry correlate accurately with values obtained by solution methods.
Protein science : a publication of the Protein Society 2006;15(6):1465-75.
2006: Sivaraman Sharada; Kirsch Jack F
The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II.
The FEBS journal 2006;273(9):1920-9.
2005: Capitani Guido; Tschopp Markus; Eliot Andrew C; Kirsch Jack F; Grütter Markus G
Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine.
FEBS letters 2005;579(11):2458-62.
2005: Aitken Susan M; Kirsch Jack F
The enzymology of cystathionine biosynthesis: strategies for the control of substrate and reaction specificity.
Archives of biochemistry and biophysics 2005;433(1):166-75.
2004: Chow Margaret A; McElroy Kathryn E; Corbett Kevin D; Berger James M; Kirsch Jack F
Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase.
Biochemistry 2004;43(40):12780-7.
2004: McCarter John D; Stephens Daren; Shoemaker Kevin; Rosenberg Steve; Kirsch Jack F; Georgiou George
Substrate specificity of the Escherichia coli outer membrane protease OmpT.
Journal of bacteriology 2004;186(17):5919-25.
2004: Rothman Steven C; Voorhies Mark; Kirsch Jack F
Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.
Protein science : a publication of the Protein Society 2004;13(3):763-72.
2004: Aitken Susan M; Kirsch Jack F
Role of active-site residues Thr81, Ser82, Thr85, Gln157, and Tyr158 in yeast cystathionine beta-synthase catalysis and reaction specificity.
Biochemistry 2004;43(7):1963-71.
2004: Sandmark Jenny; Eliot Andrew C; Famm Kristoffer; Schneider Gunter; Kirsch Jack F
Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.
Biochemistry 2004;43(5):1213-22.
2004: Ko SaeHee; Eliot Andrew C; Kirsch Jack F
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase.
Archives of biochemistry and biophysics 2004;421(1):85-90.
2004: Eliot Andrew C; Kirsch Jack F
Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Annual review of biochemistry 2004;73():383-415.
2003: Eliot Andrew C; Kirsch Jack F
Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selection.
Accounts of chemical research 2003;36(10):757-65.
2003: Aitken Susan M; Kim Daniel H; Kirsch Jack F
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions.
Biochemistry 2003;42(38):11297-306.
2003: Capitani Guido; Eliot Andrew C; Gut Heinz; Khomutov Radii M; Kirsch Jack F; Grütter Markus G
Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
Biochimica et biophysica acta 2003;1647(1-2):55-60.
2003: Rothman Steven C; Kirsch Jack F
How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase.
Journal of molecular biology 2003;327(3):593-608.
2003: Aitken Susan M; Kirsch Jack F
Kinetics of the yeast cystathionine beta-synthase forward and reverse reactions: continuous assays and the equilibrium constant for the reaction.
Biochemistry 2003;42(2):571-8.
2002: Shaffer Wendy A; Luong Tinh N; Rothman Steven C; Kirsch Jack F
Quantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase.
Protein science : a publication of the Protein Society 2002;11(12):2848-59.
2002: Capitani Guido; McCarthy Darla L; Gut Heinz; Grütter Markus G; Kirsch Jack F
Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
The Journal of biological chemistry 2002;277(51):49735-42.
2002: Kenyon George L; DeMarini David M; Fuchs Elaine; Galas David J; Kirsch Jack F; Leyh Thomas S; Moos Walter H; Petsko Gregory A; Ringe Dagmar; Rubin Gerald M; Sheahan Laura C;
Defining the mandate of proteomics in the post-genomics era: workshop report.
Molecular & cellular proteomics : MCP 2002;1(10):763-80.
2002: Eliot Andrew C; Sandmark Jenny; Schneider Gunter; Kirsch Jack F
The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation.
Biochemistry 2002;41(42):12582-9.
2002: Pons Jaume; Stratton Jennifer R; Kirsch Jack F
How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?
Protein science : a publication of the Protein Society 2002;11(10):2308-15.
2002: Deu Edgar; Koch Keith A; Kirsch Jack F
The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants.
Protein science : a publication of the Protein Society 2002;11(5):1062-73.
2002: Eliot Andrew C; Kirsch Jack F
Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.
Biochemistry 2002;41(11):3836-42.
2001: McCarthy D L; Capitani G; Feng L; Gruetter M G; Kirsch J F
Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.
Biochemistry 2001;40(41):12276-84.
2001: Stratton J R; Pelton J G; Kirsch J F
A novel engineered subtilisin BPN' lacking a low-barrier hydrogen bond in the catalytic triad.
Biochemistry 2001;40(35):10411-6.
2001: Koch K A; Capitani G; Gruetter M G; Kirsch J F
The human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-carboxylate synthase encodes a protein lacking that activity.
Gene 2001;272(1-2):75-84.
2001: Luong T N; Kirsch J F
A general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular association.
Protein science : a publication of the Protein Society 2001;10(3):581-91.
2000: Feng L; Geck M K; Eliot A C; Kirsch J F
Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase.
Biochemistry 2000;39(49):15242-9.
2000: 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 2000;40(1):49-57.
2000: 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 2000;39(10):2436-44.
1999: Capitani G; Hohenester E; Feng L; Storici P; Kirsch J F; 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 1999;294(3):745-56.
1999: Geck M K; Kirsch J F
A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system.
Biochemistry 1999;38(25):8032-7.
1999: Pons J; Rajpal A; 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 : a publication of the Protein Society 1999;8(5):958-68.
1998: Rajpal A; Taylor M G; Kirsch J F
Quantitative evaluation of the chicken lysozyme epitope in the HyHEL-10 Fab complex: free energies and kinetics.
Protein science : a publication of the Protein Society 1998;7(9):1868-74.
1998: Taylor M G; Rajpal A; Kirsch J F
Kinetic epitope mapping of the chicken lysozyme.HyHEL-10 Fab complex: delineation of docking trajectories.
Protein science : a publication of the Protein Society 1998;7(9):1857-67.
1997: Li Y; Feng L; Kirsch J F
Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase.
Biochemistry 1997;36(49):15477-88.
1997: Luong T N; Kirsch J F
A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acids.
Analytical biochemistry 1997;253(1):46-9.
1997: Park Y; Luo J; Schultz P G; Kirsch J F
Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism.
Biochemistry 1997;36(34):10517-25.
1996: Ramjee M K; Petithory J R; McElver J; Weber S C; Kirsch J F
A novel yeast expression/secretion system for the recombinant plant thiol endoprotease propapain.
Protein engineering 1996;9(11):1055-61.
1996: Wolf A; Lee K C; Kirsch J F; Ames G F
Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity.
The Journal of biological chemistry 1996;271(35):21243-50.
1996: Goldberg J M; 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 1996;35(16):5280-91.
1996: Gloss L M; Spencer D E; 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 1996;24(2):195-208.
1996: Matsumura I; Kirsch J F
Synergistic contributions of asparagine 46 and aspartate 52 to the catalytic mechanism of chicken egg white lysozyme.
Biochemistry 1996;35(6):1890-6.
1996: Matsumura I; Kirsch J F
Is aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis.
Biochemistry 1996;35(6):1881-9.
1995: Shih P; Kirsch J F
Design and structural analysis of an engineered thermostable chicken lysozyme.
Protein science : a publication of the Protein Society 1995;4(10):2063-72.
1995: Shih P; Holland D R; Kirsch J F
Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules.
Protein science : a publication of the Protein Society 1995;4(10):2050-62.
1995: Onuffer J J; 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 : a publication of the Protein Society 1995;4(9):1750-7.
1995: Onuffer J J; Ton B T; Klement I; Kirsch J F
The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.
Protein science : a publication of the Protein Society 1995;4(9):1743-9.
1995: Gloss L M; 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 1995;34(38):12323-32.
1995: Malashkevich V N; Onuffer J J; Kirsch J F; Jansonius J N
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Nature structural biology 1995;2(7):548-53.
1995: Furumo N C; Kirsch J F
Accumulation of the quinonoid intermediate in the reaction catalyzed by aspartate aminotransferase with cysteine sulfinic acid.
Archives of biochemistry and biophysics 1995;319(1):49-54.
1995: Gloss L M; Kirsch J F
Use of site-directed mutagenesis and alternative substrates to assign the prototropic groups important to catalysis by Escherichia coli aspartate aminotransferase.
Biochemistry 1995;34(12):3999-4007.
1995: Gloss L M; Kirsch J F
Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine.
Biochemistry 1995;34(12):3990-8.
1994: White M F; Vasquez J; Yang S F; Kirsch J F
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.
Proceedings of the National Academy of Sciences of the United States of America 1994;91(26):12428-32.
1994: Hohenester E; White M F; Kirsch J F; 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.
Journal of molecular biology 1994;243(5):947-9.
1994: Onuffer J J; Kirsch J F
Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change.
Protein engineering 1994;7(3):413-24.
1993: Goldberg J M; Zheng J; Deng H; Chen Y Q; Callender R; Kirsch J F
Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy.
Biochemistry 1993;32(32):8092-7.
1993: Kam-Morgan L N; Smith-Gill S J; Taylor M G; Zhang L; Wilson A C; Kirsch J F
High-resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site-directed mutagenesis.
Proceedings of the National Academy of Sciences of the United States of America 1993;90(9):3958-62.
1993: Toney M D; Kirsch J F
Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift.
Biochemistry 1993;32(6):1471-9.
1993: Shih P; Malcolm B A; Rosenberg S; Kirsch J F; Wilson A C
Reconstruction and testing of ancestral proteins.
Methods in enzymology 1993;224():576-90.
1993: Kam-Morgan L N; Lavoie T B; Smith-Gill S J; Kirsch J F
Site-directed mutagenesis in analysis of protein-protein interactions.
Methods in enzymology 1993;224():503-16.
1992: Gloss L M; Planas A; Kirsch J F
Contribution to catalysis and stability of the five cysteines in Escherichia coli aspartate aminotransferase. Preparation and properties of a cysteine-free enzyme.
Biochemistry 1992;31(1):32-9.
1992: Toney M D; Kirsch J F
Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant.
Protein science : a publication of the Protein Society 1992;1(1):107-19.
1991: Toney M D; Kirsch J F
The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate.
The Journal of biological chemistry 1991;266(35):23900-3.
1991: Petithory J R; Masiarz F R; Kirsch J F; Santi D V; Malcolm B A
A rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus.
Proceedings of the National Academy of Sciences of the United States of America 1991;88(24):11510-4.
1991: Planas A; Kirsch J F
Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine.
Biochemistry 1991;30(33):8268-76.
1991: Toney M D; Kirsch J F
Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase.
Biochemistry 1991;30(30):7461-6.
1991: Toney M D; Kirsch J F
Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase.
Biochemistry 1991;30(30):7456-61.
1991: Goldberg J M; Swanson R V; Goodman H S; Kirsch J F
The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.
Biochemistry 1991;30(1):305-12.
1990: Planas A; Kirsch J F
Sequential protection-modification method for selective sulfhydryl group derivatization in proteins having more than one cysteine.
Protein engineering 1990;3(7):625-8.
1990: Malcolm B A; Wilson K P; Matthews B W; Kirsch J F; Wilson A C
Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing.
Nature 1990;345(6270):86-9.
1990: Kirsch J F; Toney M D
Brønsted analysis of enzymatic proton transfer reactions through site-directed mutagenesis.
Annals of the New York Academy of Sciences 1990;585():48-57.
1989: Julin D A; Wiesinger H; Toney M D; Kirsch J F
Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids with solvent.
Biochemistry 1989;28(9):3815-21.
1989: McLeish M J; Julin D A; Kirsch J F
Aspartate aminotransferase catalyzed oxygen exchange with solvent from oxygen-18-enriched alpha-ketoglutarate: evidence for slow exchange of enzyme-bound water.
Biochemistry 1989;28(9):3821-5.
1989: Julin D A; Kirsch J F
Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism.
Biochemistry 1989;28(9):3825-33.
1989: Toney M D; Kirsch J F
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines.
Science (New York, N.Y.) 1989;243(4897):1485-8.
1989: Hardy L W; Kirsch J F
Isolation of a Staphylococcus aureus beta-lactamase-dicloxacillin complex and kinetic studies on the reactivation of the enzyme.
Archives of biochemistry and biophysics 1989;268(1):338-48.
1989: Malcolm B A; Rosenberg S; Corey M J; Allen J S; de Baetselier A; Kirsch J F
Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme.
Proceedings of the National Academy of Sciences of the United States of America 1989;86(1):133-7.
1988: Cronin C N; Kirsch J F
Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.
Biochemistry 1988;27(12):4572-9.
1987: Toney M D; Kirsch J F
Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. A site-directed mutagenesis study.
The Journal of biological chemistry 1987;262(26):12403-5.
1987: Kochhar S; Finlayson W L; Kirsch J F; Christen P
The stereospecific labilization of the C-4' pro-S hydrogen of pyridoxamine 5'-phosphate is abolished in (Lys258----Ala) aspartate aminotransferase.
The Journal of biological chemistry 1987;262(24):11446-8.
1987: Kirsch J F
Analysis of site-directed mutagenesis experiments by linear free energy relationships.
Protein engineering 1987;1(3):148-50.
1986: Smith D L; Ringe D; Finlayson W L; Kirsch J F
Preliminary X-ray data for aspartate aminotransferase from Escherichia coli.
Journal of molecular biology 1986;191(2):301-2.
1986: Bazelyansky M; Robey E; Kirsch J F
Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase.
Biochemistry 1986;25(1):125-30.
1985: Malcolm B A; Kirsch J F
Site-directed mutagenesis of aspartate aminotransferase from E. coli.
Biochemical and biophysical research communications 1985;132(3):915-21.
1984: Jansonius J N; Eichele G; Ford G C; Kirsch J F; Picot D; Thaller C; Vincent M G; Gehring H; Christen P
Three-dimensional structure of mitochondrial aspartate aminotransferase and some functional derivatives: implications for its mode of action.
Biochemical Society transactions 1984;12(3):424-7.
1984: Kirsch J F; Eichele G; Ford G C; Vincent M G; Jansonius J N; Gehring H; Christen P
Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure.
Journal of molecular biology 1984;174(3):497-525.
1984: Hardy L W; Kirsch J F
pH dependence and solvent deuterium oxide kinetic isotope effects on Bacillus cereus beta-lactamase I catalyzed reactions.
Biochemistry 1984;23(6):1282-7.
1984: Hardy L W; Kirsch J F
Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase I.
Biochemistry 1984;23(6):1275-82.
1984: Hardy L W; Nishida C H; Kirsch J F
Anomalous pH dependence of the reactions of carbenicillin and sulbenicillin with Bacillus cereus beta-lactamase I. Influence of the alpha-substituent charge on the kinetic parameters.
Biochemistry 1984;23(6):1288-94.
1984: Jansonius J N; Eichele G; Ford G C; Kirsch J F; Picot D; Thaller C; Vincent M G; Gehring H; Christen P
Crystallographic studies on the mechanism of action of mitochondrial aspartate aminotransferase.
Progress in clinical and biological research 1984;144B():195-203.
1982: Brouwer A C; Kirsch J F
Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation.
Biochemistry 1982;21(6):1302-7.
1981: Rosenberg S; Kirsch J F
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysis.
Biochemistry 1981;20(11):3196-204.
1981: Rosenberg S; Kirsch J F
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 1. beta-galactosidease-catalyzed hydrolysis.
Biochemistry 1981;20(11):3189-96.
1980: Thomas R A; Kirsch J F
Kinetics and mechanism of inhibition of Escherichia coli alkaline phosphatase by permanganate ion.
Biochemistry 1980;19(23):5328-34.

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