E. Kantrowitz

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Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase

Patrice Vachette, Evan R Kantrowitz, Luc Fetler, 2007, Proceedings of the National Academy of Sciences.

The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site‐specific mutagenesis

E. Kantrowitz, K. Holtz, 1999, FEBS letters.

A revised mechanism for the alkaline phosphatase reaction involving three metal ions.

B. Stec, E. Kantrowitz, K. Holtz, 2000, Journal of molecular biology.

The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites.

E. Kantrowitz, Y. Zhang, 1991, The Journal of biological chemistry.

Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis.

E. Kantrowitz, Y. Zhang, 1992, Biochemistry.

Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase

Boguslaw Stec, Evan R. Kantrowitz, C. Macol, 2001, Nature Structural Biology.

The Role of Intersubunit Interactions for the Stabilization of the T State of Escherichia coli Aspartate Transcarbamoylase*

C. Macol, H. Tsuruta, E. Kantrowitz, 2002, The Journal of Biological Chemistry.

Importance of Domain Closure for the Catalysis and Regulation ofEscherichia coli Aspartate Transcarbamoylase*

C. Macol, H. Tsuruta, E. Kantrowitz, 2002, The Journal of Biological Chemistry.

Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

E. Kantrowitz, S. Nowlan, 1985, The Journal of biological chemistry.

Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, W. Xu, J. Stebbins, 1989, Biochemistry.

The Contribution of Individual Interchain Interactions to the Stabilization of the T and R States of Escherichia coliAspartate Transcarbamoylase*

E. Kantrowitz, J. B. Sakash, Jessica B. Sakash, 2000, The Journal of Biological Chemistry.

Three of the Six Possible Intersubunit Stabilizing Interactions Involving Glu-239 Are Sufficient for Restoration of the Homotropic and Heterotropic Properties of Escherichia coliAspartate Transcarbamoylase*

H. Tsuruta, E. Kantrowitz, R. S. Chan, 2000, The Journal of Biological Chemistry.

Characterization of a Monomeric Escherichia coli Alkaline Phosphatase Formed upon a Single Amino Acid Substitution*

E. Kantrowitz, R. R. Boulanger, 2003, Journal of Biological Chemistry.

Reaction of Woodward's Reagent K with pancreatic porcine phospholipase A2: modification of an essential carboxylase residue.

E. Kantrowitz, J. Hajdu, D. Dinur, 1981, Biochemical and biophysical research communications.

Evidence for an active T‐state pig kidney fructose 1,6‐bisphosphatase: Interface residue Lys‐42 is important for allosteric inhibition and AMP cooperativity

B. Stec, E. Kantrowitz, E. Giroux, 1996, Protein science : a publication of the Protein Society.

Probing the role of histidine-372 in zinc binding and the catalytic mechanism of Escherichia coli alkaline phosphatase by site-specific mutagenesis.

E. Kantrowitz, X. Xu, X. Qin, 1994, Biochemistry.

Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.

E. Kantrowitz, J. Murphy, T. Tibbitts, 1996, Journal of molecular biology.

Escherichia coli alkaline phosphatase: X‐ray structural studies of a mutant enzyme (His‐412 → Asn) at one of the catalytically important zinc binding sites

E. Kantrowitz, T. Tibbitts, L. Ma, 1995, Protein science : a publication of the Protein Society.

Glutamic acid residues as metal ligands in the active site of Escherichia coli alkaline phosphatase.

E. Kantrowitz, C. Wojciechowski, 2003, Biochimica et biophysica acta.

Structural consequences of a one atom mutation on aspartate transcarbamylase from E. coli

J. Cherfils, R. Sweet, E. Kantrowitz, 1989, FEBS letters.

Use of L‐asparagine and N‐phosphonacetyl‐L‐asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbomoylase

H. Tsuruta, E. Kantrowitz, J. Eldo, 2008, Proteins.

Domain Bridging Interactions

H. Tsuruta, E. Kantrowitz, M. K. Williams, 2001, The Journal of Biological Chemistry.

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, S. Middleton, J. Stebbins, 1989, Biochemistry.

Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, S. Middleton, 1988, Biochemistry.

Propagation of allosteric changes through the catalytic-regulatory interface of Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, W. Xu, S. Middleton, 1988, Biochemistry.

Involvement of tryptophan 209 in the allosteric interactions of Escherichia coli aspartate transcarbamylase using single amino acid substitution mutants.

E. Kantrowitz, S. Middleton, K. Smith, 1986, Journal of molecular biology.

Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, Y. Zhang, J. Stebbins, 1990, Biochemistry.

Altering of the Metal Specificity of Escherichia coliAlkaline Phosphatase*

E. Kantrowitz, C. Wojciechowski, 2002, The Journal of Biological Chemistry.

E. coli aspartate transcarbamylase: Part II: Structure and allosteric interactions

W. Lipscomb, E. Kantrowitz, S. Pastra-Landis, 1980 .

N-phosphonacetyl-L-isoasparagine a Potent and Specific Inhibitor of E. coli Aspartate Transcarbamoylase †

E. Kantrowitz, J. Eldo, J. Cardia, 2008 .

Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, W. Xu, Wei Xu, 1989, Biochemistry.

Identification of a trans-acting regulatory factor involved in the control of the pyrimidine pathway in E. coli

E. Kantrowitz, S. Nowlan, 2004, Molecular and General Genetics MGG.

Direct observation of an altered quaternary‐structure transition in a mutant aspartate transcarbamoylase

H. Tsuruta, E. Kantrowitz, P. Vachette, 1998, Proteins.

L-Aspartate Association Contributes to Rate Limitation and Induction of the T → R Transition in Escherichia coli Aspartate Transcarbamoylase

E. Kantrowitz, B. Lee, M. O'Leary, 1995, The Journal of Biological Chemistry.

Arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site‐specific mutagenesis, NMR, and X‐ray crystallographic study

D. E. Robertson, R. Stevens, W. Lipscomb, 1992, Protein science : a publication of the Protein Society.

Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, P. Vachette, P. Tauc, 1990, Journal of molecular biology.

Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, C. Newton, N. J. Dembowski, 1990, Biochemistry.

Affinity and hydrophobic chromatography of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, T. West, I. Maldonado, 1985, Biochimica et biophysica acta.

Comparison of the essential arginine residue in Escherichia coli ornithine and aspartate transcarbamylases.

E. Kantrowitz, J. Hauber, A. Fortin, 1981, Biochimica et biophysica acta.

E. coli aspartate transcarbamylase: Part I: Catalytic and regulatory functions

W. Lipscomb, E. Kantrowitz, S. Pastra-Landis, 1980 .

The interaction of tetraiodofluorescein with aspartate transcarbamylase.

W. Lipscomb, E. Kantrowitz, C. McMurray, 1973, Biochemical and biophysical research communications.

An essential arginine residue in porcine phospholipiase A2.

E. Kantrowitz, L. A. Vensel, 1980, The Journal of biological chemistry.

Arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site‐specific mutagenesis, NMR, and X‐ray crystallographic study

D. E. Robertson, R C Stevens, R. Stevens, 1992, Protein science : a publication of the Protein Society.

The road less travelled: taming phosphatases.

B. Stec, E. Kantrowitz, T. Widlanski, 1997, Chemistry & biology.

Amino acid substitutions at the subunit interface of dimeric escherichia coli alkaline phosphatase cause reduced structural stability

E. Kantrowitz, S. Pastra-Landis, Donna Carolan Martin, 1999, Protein science : a publication of the Protein Society.

Room temperature phosphorescence study of phosphate binding in Escherichia coli alkaline phosphatase.

L. Sun, E. Kantrowitz, W. Galley, 1997, European journal of biochemistry.

Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism.

E. Kantrowitz, X. Xu, 1993, Biochemistry.

Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis.

E. Kantrowitz, J. Murphy, A. Chaidaroglou, 1993, Biochemistry.

Design, synthesis, and bioactivity of novel inhibitors of E. coli aspartate transcarbamoylase.

E. Kantrowitz, J. Eldo, Sabrina Heng, 2007, Bioorganic & medicinal chemistry letters.

A library of novel allosteric inhibitors against fructose 1,6-bisphosphatase.

E. Kantrowitz, Kimberly R Gryncel, S. Heng, 2009, Bioorganic & medicinal chemistry.

Structure and mechanisms of Escherichia coli aspartate transcarbamoylase.

Evan R Kantrowitz, W. Lipscomb, E. Kantrowitz, 2012, Accounts of chemical research.

E. coli Alkaline Phosphatase

E. Kantrowitz, 2006 .

The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase

E. Kantrowitz, J. B. Sakash, Anita Tsen, 2008, Protein science : a publication of the Protein Society.

Submicromolar phosphinic inhibitors of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, J. Montchamp, L. Coudray, 2009, Bioorganic & medicinal chemistry letters.

A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase.

L. Sun, W. Lipscomb, E. Kantrowitz, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Alternate modes of binding in two crystal structures of alkaline phosphatase‐inhibitor complexes

B. Stec, E. Kantrowitz, T. Widlanski, 2000, Protein science : a publication of the Protein Society.

T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition.

E. Kantrowitz, J. Eldo, J. Cardia, 2006, Biochemistry.

Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase.

E. Kantrowitz, S. Middleton, A. Chaidaroglou, 1988, Biochemistry.

Interaction of tetraiodofluorescein with aspartate transcarbamylase and its isolated catalytic and regulatory subunits.

W. Lipscomb, E. Kantrowitz, L. B. Jacobsverg, 1975, The Journal of biological chemistry.

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N‐phosphonacetyl‐L‐aspartate at 2.1 Å

W. Lipscomb, B. Stec, E. Kantrowitz, 1999, Proteins.

The influence of the regulatory chain amino acids Glu-62 and IIe-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, M. Dutta, 1998, Biochemistry.

The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects.

E. Kantrowitz, J. B. Sakash, 1998, Biochemistry.

Escherichia coli aspartate transcarbamylase: the relation between structure and function.

W. Lipscomb, E. Kantrowitz, 1988, Science.

Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.

E. Kantrowitz, J. Murphy, T. Tibbitts, 1995, Journal of molecular biology.

A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activity.

E. Kantrowitz, X. Xu, 1991, Biochemistry.

Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors.

B. Stec, E. Kantrowitz, K. Stieglitz, 2007, Acta crystallographica. Section D, Biological crystallography.

Crystallization and structure determination of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase.

E. Kantrowitz, J. Vitali, G. Webster, 2000, Acta crystallographica. Section D, Biological crystallography.

Characterization of the Aspartate Transcarbamoylase fromMethanococcus jannaschii *

C. Macol, E. Kantrowitz, G. Hervé, 2000, The Journal of Biological Chemistry.

Replacement of Asp‐162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase

C. Macol, L. Fetler, E. Kantrowitz, 2002, Protein science : a publication of the Protein Society.

aspartate transcarbamoylasecoli E . substrates while enhancing the effect of the allosteric activator ATP on Replacement of Asp-162 by Ala prevents the cooperative transition by the

C. Macol, D. Baker, L. Fetler, 2002 .

Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, S. Middleton, M. Ladjimi, 1988, Biochemistry.

Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementation.

E. Kantrowitz, J. Murphy, M. J. Hehir, 2000, Journal of molecular biology.

Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.

B. Stec, E. Kantrowitz, C. Brennan, 1998, Journal of molecular biology.

of the catalytically important zinc binding sites

E. Kantrowitz, T. Tibbitts, Lan Ma, 1995 .

Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp‐369 → Asn): A mechanism involving one zinc per active site

E. Kantrowitz, T. Tibbitts, Xu Xu, 1994, Protein science : a publication of the Protein Society.

Trapping and visualization of a covalent enzyme–phosphate intermediate

Boguslaw Stec, Evan R. Kantrowitz, Lan Ma, 1997, Nature Structural Biology.

Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases?

E. Kantrowitz, Jennifer E. Murphy, 1994, Molecular microbiology.

Pyrococcus abyssi alkaline phosphatase: the dimer is the active form.

E. Kantrowitz, J. Boudrant, S. Zappa, 2004, Journal of inorganic biochemistry.

Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase.

E. Kantrowitz, J. Murphy, X. Xu, 1995, The Journal of biological chemistry.

Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase.

E. Kantrowitz, K. Stieglitz, Jie Wang, 2005, Biochemistry.

A Model of the Transition State in the Alkaline Phosphatase Reaction*

B. Stec, E. Kantrowitz, K. Holtz, 1999, The Journal of Biological Chemistry.

Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase.

P. Phelan, E. Kantrowitz, N. Kelley-Loughnane, 2002, Biochimica et biophysica acta.

Mutations at histidine 412 alter zinc binding and eliminate transferase activity in Escherichia coli alkaline phosphatase.

E. Kantrowitz, E R Kantrowitz, L Ma, 1994, The Journal of biological chemistry.

Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active center.

L. Sun, E. Kantrowitz, D. Martin, 1999, Biochemistry.

Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity

E. Kantrowitz, C. Wojciechowski, J. Cardia, 2002, Protein science : a publication of the Protein Society.

The Ala-161-->Thr substitution in Escherichia coli alkaline phosphatase does not result in loss of enzymatic activity although the homologous mutation in humans causes hypophosphatasia.

E. Kantrowitz, A. Chaidaroglou, 1993, Biochemical and biophysical research communications.

Overexpression and purification of the trimeric aspartate transcarbamoylase from Bacillus subtilis.

D. Baker, E. Kantrowitz, M. K. Williams, 1995, Protein expression and purification.

Mechanism of thermal decomposition of carbamoyl phosphate and its stabilization by aspartate and ornithine transcarbamoylases

V. Guallar, E. Kantrowitz, Qin Wang, 2008, Proceedings of the National Academy of Sciences.

Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine

E. Kantrowitz, Jie Wang, 2006, Protein science : a publication of the Protein Society.

The first high pH structure of Escherichia coli aspartate transcarbamoylase

E. Kantrowitz, K. Stieglitz, Jiarong Xia, 2009, Proteins.

Use of silicate sol-gels to trap the R and T quaternary conformational states of pig kidney fructose-1,6-bisphosphatase.

E. Kantrowitz, J. McIninch, 2001, Biochimica et biophysica acta.

Functionally important arginine residues of aspartate transcarbamylase.

W. Lipscomb, E. Kantrowitz, 1977, The Journal of biological chemistry.

Importance of the Dimer-Dimer Interface for Allosteric Signal Transduction and AMP Cooperativity of Pig Kidney Fructose-1,6-Bisphosphatase

E. Kantrowitz, E. Giroux, G. Lu, 1997, The Journal of Biological Chemistry.

Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase.

H. Rabitz, Genyuan Li, J. Rabinowitz, 2008, Biochemistry.

Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanism.

J. Gouaux, W. Lipscomb, E. Kantrowitz, 1989, Biochemistry.

A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.

E. Kantrowitz, M. Ladjimi, 1988, Biochemistry.

New paradigm for allosteric regulation of Escherichia coli aspartate transcarbamoylase.

Wenyue Guo, Gregory M Cockrell, Evan R Kantrowitz, 2013, Biochemistry.

Metal ion involvement in the allosteric mechanism of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, G. Cockrell, 2012, Biochemistry.

A second allosteric site in Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, G. Cockrell, A. W. Peterson, 2012, Biochemistry.

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase.

Evan R Kantrowitz, E. Kantrowitz, 2012, Archives of biochemistry and biophysics.

Asymmetric allosteric signaling in aspartate transcarbamoylase.

E. Kantrowitz, K. Mendes, J. Martinez, 2010, ACS chemical biology.

A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure.

B. Stec, E. Kantrowitz, M. K. Williams, 1998, Journal of molecular biology.

Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATP.

E. Kantrowitz, Y. Zhang, Yang Zhang, 1989, Biochemistry.

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition.

W. Lipscomb, E. Kantrowitz, 1990, Trends in biochemical sciences.

A Fluorescent Probe-labeled Escherichia coli Aspartate Transcarbamoylase That Monitors the Allosteric Conformational State*

H. Tsuruta, E. Kantrowitz, Jay M. West, 2004, Journal of Biological Chemistry.

Designing inhibitors against fructose 1,6-bisphosphatase: exploring natural products for novel inhibitor scaffolds.

E. Kantrowitz, Katharine M. Harris, S. Heng, 2010, European journal of medicinal chemistry.

The importance of aspartate 327 for catalysis and zinc binding in Escherichia coli alkaline phosphatase.

E. Kantrowitz, X. Xu, Xu Xu, 1992, The Journal of biological chemistry.

Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.

E. Kantrowitz, C. Newton, Colin J. Newton, 1990, Biochemistry.

The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase.

D. Baker, E. Kantrowitz, 1993, Biochemistry.

Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase.

W. Lipscomb, L. Kuo, E. Kantrowitz, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states.

B. Stec, D. Baker, E. Kantrowitz, 2004, Journal of molecular biology.

Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis.

R. Stevens, W. Lipscomb, Y. Chook, 1991, Protein engineering.

Crystal structures of the active site mutant (Arg‐243 → Ala) in the T and R allosteric states of pig kidney fructose‐1,6‐bisphosphatase expressed in escherichia coli

B. Stec, E. Kantrowitz, E. Giroux, 1996, Protein science : a publication of the Protein Society.

Conversion of the noncooperative Bacillus subtilis aspartate transcarbamoylase into a cooperative enzyme by a single amino acid substitution.

E. Kantrowitz, J. Stebbins, 1992, Biochemistry.

An improved colorimetric assay for aspartate and ornithine transcarbamylases.

E. Kantrowitz, J. Foote, S. Pastra-Landis, 1981, Analytical biochemistry.

Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase

Wenyue Guo, Evan R Kantrowitz, H. Tsuruta, 2012, Proceedings of the National Academy of Sciences.

A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.

H. Tsuruta, E. Kantrowitz, K. Stieglitz, 2005, Journal of molecular biology.

240s Loop Interactions Stabilize the T State of Escherichia coli Aspartate Transcarbamoylase*

H. Tsuruta, E. Kantrowitz, S. Gourinath, 2004, Journal of Biological Chemistry.

Stabilization of the R Allosteric Structure of Escherichia coli Aspartate Transcarbamoylase by Disulfide Bond Formation*

H. Tsuruta, E. Kantrowitz, Jay M. West, 2002, The Journal of Biological Chemistry.

Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, M. K. Williams, 1998, Biochimica et biophysica acta.

Glu‐50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure

E. Kantrowitz, P. Vachette, P. Tauc, 1994, Protein science : a publication of the Protein Society.

Crystal structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase

E. Kantrowitz, J. Vitali, M. Colaneri, 2008, Proteins.

Domain Closure in the Catalytic Chains of Escherichia coli Aspartate Transcarbamoylase Influences the Kinetic Mechanism (*)

E. Kantrowitz, M. O'Leary, F. Wedler, 1995, The Journal of Biological Chemistry.

Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, W. Xu, 1991, Biochemistry.

Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme.

Boguslaw Stec, Evan R Kantrowitz, B. Stec, 2005, Acta crystallographica. Section D, Biological crystallography.

Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.

R. Stevens, E. Kantrowitz, C. Newton, 1992, Biochemistry.

A cooperative Escherichia coli aspartate transcarbamoylase without regulatory subunits .

E. Kantrowitz, K. Mendes, 2010, Biochemistry.

Glutamic acid residue 98 is critical for catalysis in pig kidney fructose-1,6-bisphosphatase.

E. Kantrowitz, E. Giroux, G. Lu, 1996, Biochemical and Biophysical Research Communications - BBRC.

Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition.

E. Kantrowitz, M. K. Williams, E. Giroux, 1994, The Journal of biological chemistry.

Crystallographic snapshots of the complete catalytic cycle of the unregulated aspartate transcarbamoylase from Bacillus subtilis.

E. Kantrowitz, D. Puleo, G. Cockrell, 2011, Journal of molecular biology.

AMP inhibition of pig kidney fructose-1,6-bisphosphatase.

E. Kantrowitz, N. Kelley-Loughnane, 2001, Biochimica et biophysica acta.

Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions.

E. Kantrowitz, J. Daigneault, R. Silver, 1983, Journal of molecular biology.

Analysis of mutant Escherichia coli aspartate transcarbamylases isolated from a series of suppressed pyrB nonsense strains.

E. Kantrowitz, R. Ferraro, J. Daigneault, 1981, Journal of molecular biology.

Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases.

E. Kantrowitz, A. Hengge, K. Holtz, 2000, Biochemistry.

Alteration of aspartate 101 in the active site of Escherichia coli alkaline phosphatase enhances the catalytic activity.

E. Kantrowitz, A. Chaidaroglou, 1989, Protein engineering.

Ultraviolet photochemistry of formatopentaamminecobalt(III) ion in aqueous solution. Hydrogen atom formation and oxygen .far. carbon linkage isomerization

E. Kantrowitz, M. Hoffman, Kenneth M. Schilling, 1972 .

Photolytically induced oxygen.far.carbon linkage isomerization in formato- and oxalatoamine complexes of cobalt(III)

E. Kantrowitz, M. Hoffman, Anthony F. Vaudo, 1971 .

Ultraviolet photochemistry of acetatopentaamminecobalt(III) in aqueous solution

E. Kantrowitz, M. Hoffman, J. Endicott, 1971 .

Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.

E. Kantrowitz, J. Cardia, K. Stieglitz, 2005, Proceedings of the National Academy of Sciences of the United States of America.

The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity

C. Macol, B. Stec, H. Tsuruta, 1999, Protein science : a publication of the Protein Society.

N-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase.

H. Tsuruta, E. Kantrowitz, J. Eldo, 2006, Journal of medicinal chemistry.

Catalytic-regulatory subunit interactions and allosteric effects in aspartate transcarbamylase.

E. Kantrowitz, M. Ladjimi, 1987, The Journal of biological chemistry.

An essential residue at the active site of aspartate transcarbamylase.

W. Lipscomb, E. Kantrowitz, 1976, The Journal of biological chemistry.

Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase.

E. Kantrowitz, M. K. Williams, 1992, Proceedings of the National Academy of Sciences of the United States of America.

A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structures.

Boguslaw Stec, Evan R. Kantrowitz, E. Kantrowitz, 2000, Biochemistry.

Two spectrophotometric experiments with alpha-chymotrypsin.

E. Kantrowitz, G. Eisele, 1975, Journal of chemical education.

Time evolution of the quaternary structure of Escherichia coli aspartate transcarbamoylase upon reaction with the natural substrates and a slow, tight-binding inhibitor.

H. Tsuruta, E. Kantrowitz, Wenyue Guo, 2008, Journal of molecular biology.

Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle.

H. Tsuruta, E. Kantrowitz, J. Cardia, 2005, Journal of molecular biology.

A second allosteric site in Escherichia coli aspartate transcarbamoylase.

E. Kantrowitz, G. Cockrell, A. W. Peterson, 2012, Biochemistry.

Binding of AMP to two of the four subunits of pig kidney fructose‐1,6‐bisphosphatase induces the allosteric transition

E. Kantrowitz, N. Kelley-Loughnane, Evan R. Kantrowitz, 2001, Proteins.