P. Cook

发表

Chemical mechanism of the adenosine cyclic 3',5'-monophosphate dependent protein kinase from pH studies.

Paul Cook, M. Yoon, P. Cook, 1987, Biochemistry.

Isotope partitioning in the adenosine 3',5'-monophosphate dependent protein kinase reaction indicates a steady-state random kinetic mechanism.

P. Cook, C. Kong, 1988, Biochemistry.

Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis.

P. Cook, A. Berdis, 1993, Biochemistry.

Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis.

W. Cleland, P. Cook, R. Viola, 1979, Analytical biochemistry.

The multifaceted pyridoxal 5'-phosphate-dependent O-acetylserine sulfhydrylase.

F. Spyrakis, A. Mozzarelli, S. Bettati, 2011, Biochimica et biophysica acta.

Alpha,beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required?

P. Cook, 2003, Biochimica et biophysica acta.

O-acetylserine sulfhydrylase.

P. Cook, C. Tai, 2000, Advances in enzymology and related areas of molecular biology.

Substitution of Pyridoxal 5′-Phosphate ind-Serine Dehydratase from Escherichia coliby Cofactor Analogues Provides Information on Cofactor Binding and Catalysis*

P. Cook, C. Tai, K. Schnackerz, 1999, The Journal of Biological Chemistry.

Time-resolved fluorescence of O-acetylserine sulfhydrylase.

A. Mozzarelli, P. Cook, S. Benci, 1999, Biochimica et biophysica acta.

Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system.

Paul F Cook, P. Cook, A. West, 2005, Biochemistry.

Pyridoxal 5'-phosphate-dependent alpha,beta-elimination reactions: mechanism of O-acetylserine sulfhydrylase.

P. Cook, C. Tai, 2001, Accounts of chemical research.

Interaction of serine acetyltransferase with O‐acetylserine sulfhydrylase active site: Evidence from fluorescence spectroscopy

A. Mozzarelli, S. Bettati, P. Cook, 2005, Protein science : a publication of the Protein Society.

Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.

P. Cook, A. West, B. Andi, 2012, Biochemistry.

The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH.

P. Cook, A. West, Sang Gon Kim, 2011, Archives of biochemistry and biophysics.

Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-Å resolution

P. Cook, A. West, B. Andi, 2006, Cell Biochemistry and Biophysics.

Regulatory Mechanism of Histidine-tagged Homocitrate Synthase from Saccharomyces cerevisiae

P. Cook, A. West, B. Andi, 2005, Journal of Biological Chemistry.

Expression of Transglutaminase Substrate Activity on Candida albicans Germ Tubes through a Coiled, Disulfide-bonded N-terminal Domain of Hwp1 Requires C-terminal Glycosylphosphatidylinositol Modification*

P. Cook, Y. Bahn, J. Staab, 2004, Journal of Biological Chemistry.

Correlation between hysteresis and allosteric properties for phosphofructokinase from Ascaris suum.

H. Hofer, P. Cook, B. G. Harris, 1987, The Journal of biological chemistry.

Reaction of Ascaris suum phosphofructokinase with diethylpyrocarbonate. Inactivation and desensitization to allosteric modulation.

H. Hofer, P. Cook, B. G. Harris, 1987, The Journal of biological chemistry.

Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated.

P. Cook, B. G. Harris, G. S. Jagannatha Rao, 1999, Archives of biochemistry and biophysics.

Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.

P. Cook, A. West, K. Nicholas, 2007, Biochemistry.

Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.

Takashi Yamamoto, T. Eguchi, P. Cook, 2008, Biochemistry.

A lysine-tyrosine pair carries out acid-base chemistry in the metal ion-dependent pyridine dinucleotide-linked beta-hydroxyacid oxidative decarboxylases.

P. Cook, Deniz Aktaş, 2009, Biochemistry.

Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.

P. Cook, A. West, Ying-Wu Lin, 2009, Biochemistry.

Divergent effects of compounds on the hydrolysis and transpeptidation reactions of γ-glutamyl transpeptidase

P. Cook, Pui-Kai Li, M. Hanigan, 2012, Journal of enzyme inhibition and medicinal chemistry.

pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase.

P. Cook, D. M. Kiick, 1983, Biochemistry.

Equilibrium model in an in vitro poly(ADP-ribose) turnover system.

G. Poirier, P. Cook, A. Verreault, 1995, Biochimica et biophysica acta.

Carbohydrate substrate specificity of bacterial and plant pyrophosphate-dependent phosphofructokinases.

P. Cook, R. Voll, E. S. Younathan, 1986, Biochemistry.

Initial kinetic characterization of the multienzyme complex, cysteine synthetase

P. Cook, R. Wedding, 1977 .

A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst.

P. Cook, W. Karsten, N. M. Kredich, 1996, Biochemistry.

Effect of phorbol esters on cytosolic protein kinase C content and activity in the human monoblastoid U937 cell.

P. Cook, K. Ways, R. Riddle, 1991, The Journal of biological chemistry.

Characterization of Hwp1 from Candida albicans

P. Cook, Y. Bahn, J. Staab, 2004 .

Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase.

G. L. Kenyon, W. Cleland, P. Cook, 1981, Biochemistry.

Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme.

C. Hwang, P. Cook, W. Karsten, 1999, Biochemistry.

Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation.

P. Cook, Guangping Chen, Eduard M. Tyapochkin, 2011, Archives of biochemistry and biophysics.

para-Nitrophenyl Sulfate Activation of Human Sulfotransferase 1A1 Is Consistent with Intercepting the E·PAP Complex and Reformation of E·PAPS*

P. Cook, Guangping Chen, Eduard M. Tyapochkin, 2009, The Journal of Biological Chemistry.

Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase.

P. Cook, Guangping Chen, Eduard M. Tyapochkin, 2008, Biochemistry.

Kinetic and Chemical Mechanisms of Homocitrate Synthase from Thermus thermophilus*

P. Cook, A. West, Vidya P. Kumar, 2011, The Journal of Biological Chemistry.

Kinetic studies on the activation of pyrophosphate-dependent phosphofructokinase from mung bean by fructose 2,6-bisphosphate and related compounds.

P. Cook, R. Voll, E. S. Younathan, 1986, Biochemistry.

Purification and Properties of β-Alanine Synthase from Calf Liver

P. Cook, K. Schnackerz, G. Waldmann, 2005 .

Catalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry.

A. Mozzarelli, P. Burkhard, S. Bettati, 1998, Journal of molecular biology.

A Two-step Process Controls the Formation of the Bienzyme Cysteine Synthase Complex*

A. Mozzarelli, S. Bettati, P. Cook, 2010, The Journal of Biological Chemistry.

Evidence for a Stepwise Mechanism of OMP Decarboxylase

J. Blanchard, C. Hwang, P. Cook, 1999 .

Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction.

P. Cook, W. Rabeh, S. S. Alguindigue, 2005, Biochemistry.

The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol.

P. Cook, S. Roderick, Corey M. Johnson, 2005, Archives of biochemistry and biophysics.

Pyridoxal 5′-Phosphate-Dependent α,β-Elimination Reactions: Mechanism of O-Acetylserine Sulfhydrylase

P. Cook, C. Tai, 2001 .

pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine.

P. Cook, K. Schnackerz, S. Hara, 1992, Biochemistry.

Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae.

P. Cook, A. West, A. Vashishtha, 2009, Biochemistry.

Kinetic mechanism of dihydropyrimidine dehydrogenase from pig liver.

P. Cook, K. Schnackerz, B. Podschun, 1990, The Journal of biological chemistry.

Inhibition of human γ-glutamyl transpeptidase: development of more potent, physiologically relevant, uncompetitive inhibitors.

P. Cook, Pui-Kai Li, S. Terzyan, 2013, The Biochemical journal.

Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae.

P. Cook, S. Roderick, Bin Huang, 2008, Biochemistry.

Inverse Solvent Isotope Effects in the NAD-Malic Enzyme Reaction Are the Result of the Viscosity Difference between D2O and H2O: Implications for Solvent Isotope Effect Studies

P. Cook, W. Karsten, C. Lai, 1995 .

Bisubstrate inhibition: Theory and application to N-acetyltransferases.

J. Blanchard, P. Cook, Michael Yu, 2006, Biochemistry.

Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A.

A. Mozzarelli, S. Bettati, P. Cook, 2010, Biochemistry.

Acid-base catalytic mechanism of dihydropyrimidinase from pH studies.

Paul Cook, P. Cook, K. Schnackerz, 1993, Biochemistry.

Purification, characterization, and kinetics of porcine recombinant dihydropyrimidine dehydrogenase.

W. Hagen, F. Gonzalez, P. Cook, 1997, Protein expression and purification.

Product dependence of deuterium isotope effects in enzyme-catalyzed reactions.

M. Yoon, P. Cook, S. Hara, 1993, Biochemistry.

Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase.

P. Cook, N. E. Price, 1996, Archives of biochemistry and biophysics.

Haloacetamidine‐Based Inactivators of Protein Arginine Deiminase 4 (PAD4): Evidence that General Acid Catalysis Promotes Efficient Inactivation

P. Thompson, P. Cook, B. Knuckley, 2010, Chembiochem : a European journal of chemical biology.

Kinetics of Activated Thrombin-activatable Fibrinolysis Inhibitor (TAFIa)-catalyzed Cleavage of C-terminal Lysine Residues of Fibrin Degradation Products and Removal of Plasminogen-binding Sites*

P. Cook, J. Foley, M. Nesheim, 2011, The Journal of Biological Chemistry.

Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes.

A. Mozzarelli, P. Burkhard, S. Bettati, 2007, Biochemistry.

Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase.

N. Oppenheimer, W. Cleland, P. Cook, 1981, Biochemistry.

Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase.

P. Burkhard, Paul Cook, P. Cook, 2001, Biochemistry.

Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound.

P. Burkhard, J. Jansonius, P. Cook, 2000, Journal of molecular biology.

Structure and Mechanism of O-Acetylserine Sulfhydrylase*

P. Cook, W. Rabeh, 2004, Journal of Biological Chemistry.

A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2.

P. Cook, R. Wedding, 1976, The Journal of biological chemistry.

Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate.

P. Cook, W. Karsten, Y. Izumi, 2005, Biochemistry.

Synthesis and separation of a diastereomeric pair of phosphonopeptide inhibitors of the cyclic AMP-dependent protein kinase catalytic subunit

P. Cook, S. J. Norton, Chun-hua Yang, 1994 .

Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suum.

P. Cook, C. Kong, R. Benjamin, 1987, Archives of biochemistry and biophysics.

pH dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme.

P. Cook, B. G. Harris, S. Park, 1986, Biochemistry.

Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum.

P. Cook, B. G. Harris, J. Rao, 1985, Archives of biochemistry and biophysics.

Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rate.

P. Cook, B. L. Allen, B. G. Harris, 1984, Biochemistry.

Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum.

P. Cook, B. G. Harris, S. Park, 1984, Biochemistry.

The pH dependence of the reductive carboxylation of pyruvate by malic enzyme.

P. Cook, I. Nuiry, 1985, Biochimica et biophysica acta.

Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites.

P. Cook, W. Karsten, B. G. Harris, 2003, Biochemistry.

Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction.

F. Raushel, P. Cook, B. G. Harris, 1993, Biochemistry.

Kinetic studies to determine the mechanism of regulation of bovine liver glutamate dehydrogenase by nucleotide effectors.

P. Cook, 1982, Biochemistry.

Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme.

Paul F Cook, P. Cook, Deniz Aktaş, 2008, Biochimica et biophysica acta.

Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studies.

P. Cook, B. G. Harris, D. M. Kiick, 1986, Biochemistry.

Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.

W. Cleland, P. Cook, P. Weiss, 1991, Biochemistry.

pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase.

W. Cleland, P. Cook, W W Cleland, 1981, Biochemistry.

Kinetic mechanism and location of rate-determining steps for aspartase from Hafnia alvei.

J. Hermes, P. Cook, P. Weiss, 1984, Biochemistry.

Crystallographic Studies on Ascaris suum NAD-Malic Enzyme Bound to Reduced Cofactor and Identification of an Effector Site*

D. Coleman, P. Cook, W. Karsten, 2003, Journal of Biological Chemistry.

Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution.

E. Goldsmith, D. Coleman, P. Cook, 2002, Biochemistry.

Lysine 199 is the general acid in the NAD-malic enzyme reaction.

P. Cook, W. Karsten, D. Liu, 2000, Biochemistry.

Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis.

C. Hwang, P. Cook, W. Karsten, 1999, Biochemistry.

Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.

P. Cook, W. Karsten, 1994, Biochemistry.

Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum.

D. R. Holland, B. Finzel, S. Muchmore, 1992, Journal of Molecular Biology.

Expression, purification, and characterization of the recombinant NAD-malic enzyme from Ascaris suum.

P. Cook, W. Karsten, B. G. Harris, 1997, Protein expression and purification.

Role of the divalent metal ion in the NAD:malic enzyme reaction: An ESEEM determination of the ground state conformation of malate in the E:Mn: Malate complex

P. Cook, T. Quinn, J. Peisach, 1996, Protein science : a publication of the Protein Society.

Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum.

P. Cook, W. Karsten, S. Park, 1995, Biochemistry.

Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate.

P. Cook, C. Lai, B. G. Harris, 1992, Archives of biochemistry and biophysics.

Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate.

P. Cook, P. Weiss, B. G. Harris, 1991, Biochemistry.

Derivation of the rate equation for substrate activation by malate induced by oxalate

P. Cook, Sang Hoon Park, 1989 .

Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reaction.

P. Cook, B. G. Harris, S. Park, 1989, Biochemistry.

Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism.

P. Cook, B. G. Harris, C. Y. Chen, 1988, Biochemistry.

Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction.

P. Cook, Deniz Aktaş, 2008, Biochemistry.

Chemical mechanism of 6-phosphogluconate dehydrogenase from Candida utilis from pH studies.

P. Cook, A. Berdis, 1993, Biochemistry.

Mechanistic deductions from isotope effects in multireactant enzyme mechanisms.

W. Cleland, P. Cook, 1981, Biochemistry.

Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state.

P. Cook, B. G. Harris, G. Rao, 1991, Biochemistry.

Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers.

P. Cook, R. Wedding, 1978, The Journal of biological chemistry.

Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase.

M. A. Payne, P. Cook, B. G. Harris, 1995, Biochemistry.

Use of primary deuterium and 15N isotope effects to deduce the relative rates of steps in the mechanisms of alanine and glutamate dehydrogenases.

W. Cleland, P. Cook, P. Weiss, 1988, Biochemistry.

Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.

P. Cook, B. Bertagnolli, 1984, Biochemistry.

Adenosine cyclic 3',5'-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit.

K. Vrana, R. Roskoski, P. Cook, 1982, Biochemistry.

Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions.

W. Cleland, J. Blanchard, P. Cook, 1980, Biochemistry.

Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum malic enzyme.

P. Cook, B. G. Harris, G. Kulkarni, 1993, Archives of biochemistry and biophysics.

pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same.

W. Cleland, P. Cook, 1981, Biochemistry.

Substrate and pH Dependence of Isotope Effects in Enzyme Catalyzed Reactions

P. Cook, W. Karsten, 2005 .

Multiple isotope effects as a probe of the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate

P. Cook, W. Karsten, 2002 .

Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation.

P. Cook, B. G. Harris, S. Mallick, 1991, The Journal of biological chemistry.

The kinetic mechanism of human placental aldose reductase and aldehyde reductase II.

S. Srivastava, P. Cook, A. Bhatnagar, 1988, Archives of biochemistry and biophysics.

Enzyme Mechanism from Isotope Effects

P. Cook, 1991 .

The α-aminoadipate pathway for lysine biosynthesis in fungi

Paul F. Cook, Babak Andi, Jinghua Qian, 2006, Cell Biochemistry and Biophysics.

The alpha-aminoadipate pathway for lysine biosynthesis in fungi.

Babak Andi, Paul F Cook, Jinghua Qian, 2006, Cell biochemistry and biophysics.

Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants.

P. Cook, C. Tai, T. Jacobson, 1993, Biochemistry.

Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium.

P. Burkhard, J. Jansonius, P. Cook, 1999, Journal of molecular biology.

Isozyme-Specific Ligands for O-acetylserine sulfhydrylase, a Novel Antibiotic Target

Pietro Cozzini, Francesca Spyrakis, Paolo Benedetti, 2013, PloS one.

Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase.

Pietro Cozzini, Glen E Kellogg, Francesca Spyrakis, 2013, Biochimica et biophysica acta.

Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy.

A. Mozzarelli, S. Bettati, P. Cook, 2011, Archives of biochemistry and biophysics.

Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature.

Alexander S. Bayden, F. Spyrakis, Alessio Amadasi, 2010, Journal of medicinal chemistry.

Surface-exposed Tryptophan Residues Are Essential for O-Acetylserine Sulfhydrylase Structure, Function, and Stability*

A. Mozzarelli, S. Bettati, P. Cook, 2003, Journal of Biological Chemistry.

Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium.

P. Burkhard, Paul Cook, J. Jansonius, 1998, Journal of molecular biology.

Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies.

P. Cook, C. Tai, J. W. Simmons, 1995, Biochemistry.

Kinetic mechanism of serine transacetylase from Salmonella typhimurium.

P. Cook, L. Leu, 1994, Biochemistry.

A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium.

M. A. Payne, P. Cook, K. Schnackerz, 1990, Protein expression and purification.

(31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium.

P. Cook, K. Schnackerz, Rong-Bin Guan, 2009, Archives of biochemistry and biophysics.

Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction.

P. Cook, W. Rabeh, C. Tai, 2008, Archives of biochemistry and biophysics.

Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium.

P. Cook, W. Rabeh, C. Tai, 2008, Biochimica et biophysica acta.

Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase.

P. Cook, W. Karsten, 2002, Methods in enzymology.

Inhibition and Structural Changes of O-Acetylserine Sulfhydrylase-A from Salmonella typhimurium Upon Binding Sulfate and Chloride Anions

J. Jansonius, P. Cook, C. Tai, 2000 .

Conformational probes of O-acetylserine sulfhydrylase: fluorescence of tryptophans 50 and 161

A. Mozzarelli, S. Bettati, P. Cook, 1999 .

Substitution of Pyridoxal 5′-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides a Test of the Mechanism Proposed for Formation of the α-Aminoacrylate Intermediate*

C. Hwang, P. Cook, M. Dunn, 1996, The Journal of Biological Chemistry.

Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction.

P. Cook, C. Tai, K. Schnackerz, 1995, Biochemistry.

The Mechanism of O-Acetylserine Sulfhydrylase from Salmonella typhimurium

P. Cook, K. Schnackerz, 1994 .

Overall mechanism and rate equation for O-acetylserine sulfhydrylase.

P. Cook, R. Wedding, 1977, The Journal of biological chemistry.

Acid base catalytic mechanism of the dihydropyrimidine dehydrogenase from pH studies.

P. Cook, K. Schnackerz, B. Podschun, 1993, The Journal of biological chemistry.

A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae.

Hengyu Xu, P. Cook, A. West, 2007, Biochemistry.

Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae.

Hengyu Xu, P. Cook, A. West, 2007, Biochemistry.

Enzyme Kinetics and Mechanism

Paul F. Cook, W. Cleland, P. Cook, 2007 .

Detection of a gem-diamine and a stable quinonoid intermediate in the reaction catalyzed by serine-glyoxylate aminotransferase from Hyphomicrobium methylovorum.

P. Cook, W. Karsten, 2009, Biochimica et biophysica acta.

(31)P NMR spectroscopy senses the microenvironment of the 5'-phosphate group of enzyme-bound pyridoxal 5'-phosphate.

P. Cook, B. Andi, K. Schnackerz, 2011, Biochimica et biophysica acta.

Crystal Structure of the H256A Mutant of Rat Testis Fructose-6-phosphate,2-kinase/Fructose-2,6-bisphosphatase

H. Mizuguchi, P. Cook, K. Uyeda, 1999, The Journal of Biological Chemistry.

Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes.

P. Cook, M. Hanigan, Matthew B West, 2011, Analytical biochemistry.

A Novel, Species-specific Class of Uncompetitive Inhibitors of γ-Glutamyl Transpeptidase*

P. Cook, M. Hanigan, J. King, 2009, Journal of Biological Chemistry.

Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase.

W. Cleland, J. Hermes, P. Cook, 1987, Biochemistry.

Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues.

G. L. Kenyon, W. Cleland, P. Cook, 1988, Biochemistry.

Effects of osmolytes on the SLN1-YPD1-SSK1 phosphorelay system from Saccharomyces cerevisiae.

P. Cook, A. West, B. Andi, 2009, Biochemistry.

Reaction Mechanism of Fructose-2,6-bisphosphatase

H. Mizuguchi, P. Cook, K. Uyeda, 1999, The Journal of Biological Chemistry.

Interaction of Protein Kinase Ac from Ascaris suum with Proteins and Peptides: Comparison with the Mammalian Enzyme

R. Hoffmann, H. Hofer, P. Cook, 1997 .

Comparison of the substrate specificities of cAMP-dependent protein kinase from bovine heart and Ascaris suum muscle.

R. Hoffmann, H. Hofer, P. Cook, 1996, Biological chemistry Hoppe-Seyler.

A method for counting active sites of cyclic AMP-dependent protein kinase.

P. Cook, G. D. Mcclure, R. Qamar, 1993, Journal of enzyme inhibition.

Kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation.

M. Yoon, P. Cook, R. Qamar, 1992, Biochemistry.

Effector-induced conformational transitions in Ascaris suum phosphofructokinase. A fluorescence and circular dichroism study.

P. Cook, B. G. Harris, G. Rao, 1991, Journal of Biological Chemistry.

Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification.

P. Cook, B. G. Harris, G. Rao, 1987, The Journal of biological chemistry.

The 2′-Phosphate of NADP Is Responsible for Proper Orientation of the Nicotinamide Ring in the Oxidative Decarboxylation Reaction Catalyzed by Sheep Liver 6-Phosphogluconate Dehydrogenase*

P. Cook, Lei Li, 2006, Journal of Biological Chemistry.

Dihydropyrimidine dehydrogenase: a flavoprotein with four iron-sulfur clusters.

Y. Lindqvist, P. Cook, D. Dobritzsch, 2004, Biochimica et biophysica acta.

Molecular basis for the isozymes of bovine glucose-6-phosphate isomerase.

R. W. Gracy, P. Cook, J. Cini, 1986, Archives of biochemistry and biophysics.

Recent results and new hardware developments for protein crystal growth in microgravity

A. D. Clark, A. Sacco, K. Moore, 1994 .

Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae.

P. Cook, S. Roderick, Bin Huang, 2004, Archives of biochemistry and biophysics.

Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway.

P. Cook, G. Strambini, P. Cioni, 1996, Biochemistry.

salmonella typhimurium/enzymol.

P. Cook, R. Wedding, 1977, Archives of biochemistry and biophysics.

Lanthanide pyrophosphates as substrates for the pyrophosphate-dependent phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: evidence for a second metal ion required for reaction.

P. Cook, B. Bertagnolli, 1994, Biochemistry.

Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae.

Hengyu Xu, P. Cook, A. West, 2006, Biochemistry.

Kinetic mechanism of choline kinase from rat striata.

P. Cook, R. Reinhardt, L. Wecker, 1984, The Journal of biological chemistry.

Importance in Catalysis of the 6-Phosphate-binding Site of 6-Phosphogluconate in Sheep Liver 6-Phosphogluconate Dehydrogenase*

P. Cook, F. Dworkowski, Lei Li, 2006, Journal of Biological Chemistry.

Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae.

Paul F Cook, Jinghua Qian, Jana Khandogin, 2008, Biochemistry.

Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae.

P. Cook, A. West, B. Andi, 2004, Biochemistry.

Acid-base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae.

P. Cook, A. West, Jinghua Qian, 2006, Biochemistry.

Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae.

P. Cook, A. West, B. Andi, 2004, Archives of biochemistry and biophysics.

Regulatory Mechanism of Histidine-tagged Homocitrate Synthase from Saccharomyces cerevisiae

P. Cook, B. Andi, 2005, Journal of Biological Chemistry.

Cardiac cholinergic muscarinic receptors: changes in multiple affinity forms with down-regulation.

R. Roskoski, P. Cook, R. Reinhardt, 1985, The Journal of pharmacology and experimental therapeutics.

Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae.

P. Cook, S. Roderick, Bin Huang, 2004, Biochemistry.

Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates.

A. Mozzarelli, P. Cook, S. Benci, 1997, Biochemistry.

Resolution of pyridoxal 5'-phosphate from O-acetylserine sulfhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site.

P. Cook, K. Schnackerz, 1995, Archives of biochemistry and biophysics.

Mechanism from isotope effects.

P. Cook, 1997, Isotopes in environmental and health studies.

Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties.

J. Piškur, P. Cook, B. Andersen, 2003, Nucleic acids research.

Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae.

P. Cook, W. Karsten, Kostyantyn D. Bobyk, 2011, Archives of biochemistry and biophysics.

Initial velocity, spectral, and pH studies of the serine-glyoxylate aminotransferase from Hyphomicrobiuim methylovorum.

P. Cook, W. Karsten, Y. Izumi, 2001, Archives of biochemistry and biophysics.

Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase.

W. Cleland, P. Cook, C. Grimshaw, 1981, Biochemistry.

Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme.

P. Cook, A. West, Chao-Nan Hsu, 2015, Archives of biochemistry and biophysics.

Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.

P. Cook, A. West, Ying-Wu Lin, 2008, Biochemistry.

A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme.

P. Cook, W. Karsten, Dali Liu, 2005, Biochemistry.

Pyridine nucleotide-dependent (3-hydroxyacid oxidative decarboxylases: An overview

P. Cook, W. Karsten, 2000, Protein & Peptide Letters.

Multiple isotope effects as a probe of proton and hydride transfer in the 6-phosphogluconate dehydrogenase reaction.

C. Hwang, P. Cook, 1998, Biochemistry.

Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants.

W. Cleland, C. Hwang, P. Cook, 1998, Biochemistry.

Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis.

P. Cook, A. West, A. Vashishtha, 2015, Archives of biochemistry and biophysics.

Mechanism of the Beta-Replacement Enzyme, O-Acetylserine Sulfhydrylase

P. Cook, C. Tai, S. Nalabolu, 1991 .

Kinetic studies of the yeast His-Asp phosphorelay signaling pathway.

P. Cook, A. West, B. Andi, 2010, Methods in enzymology.

Characterization of the S272A,D Site-Directed Mutations of O-Acetylserine Sulfhydrylase: Involvement of the Pyridine Ring in the α,β-Elimination Reaction†

P. Cook, Sebastian Daum, C. Tai, 2003 .

Examination of intrinsic sulfonamide resistance in Bacillus anthracis: a novel assay for dihydropteroate synthase.

P. Cook, M. Valderas, B. Andi, 2008, Biochimica et biophysica acta.

Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction.

P. Cook, A. West, Devi K. Ekanayake, 2011, Archives of biochemistry and biophysics.

Glutamates 78 and 122 in the Active Site of Saccharopine Dehydrogenase Contribute to Reactant Binding and Modulate the Basicity of the Acid-Base Catalysts*

P. Cook, A. West, B. Andi, 2010, The Journal of Biological Chemistry.