Paul F. Cook mainly focuses on Stereochemistry, Biochemistry, Active site, Enzyme and Kinetic isotope effect. The concepts of his Stereochemistry study are interwoven with issues in Cysteine and Cysteine synthase. His studies in Active site integrate themes in fields like Pyridoxal, Schiff base, Cysteine synthase complex, Aldimine and Conformational change.
The Pyridoxal study combines topics in areas such as Tryptophan and Lysine. His Enzyme research is multidisciplinary, incorporating perspectives in Combinatorial chemistry, Racemic mixture, Catechol and Acetyltransferases. His Kinetic isotope effect research incorporates themes from Inorganic chemistry, Radiochemistry, Organic chemistry and Enzyme catalyzed.
The scientist’s investigation covers issues in Stereochemistry, Enzyme, Biochemistry, Active site and NAD+ kinase. His Stereochemistry study combines topics in areas such as Cofactor, Pyridoxal, Substrate and Kinetic isotope effect. His work in Pyridoxal addresses subjects such as Schiff base, which are connected to disciplines such as Tautomer.
In his study, which falls under the umbrella issue of Enzyme, Protein kinase A is strongly linked to Peptide. His Active site study incorporates themes from Cysteine synthase complex, Lysine, Alanine, Cysteine and Conformational change. His research in NAD+ kinase focuses on subjects like Oxidative decarboxylation, which are connected to Decarboxylation.
Paul F. Cook mostly deals with Stereochemistry, Enzyme, Biochemistry, Active site and Cysteine. He studies Conformational change which is a part of Stereochemistry. His Enzyme research incorporates elements of Protein structure and Saccharomyces cerevisiae.
His work deals with themes such as Site-directed mutagenesis, Hydrogen bond, Enzyme kinetics and Homoisocitrate dehydrogenase, which intersect with Active site. Many of his research projects under Cysteine are closely connected to Protein-arginine deiminase with Protein-arginine deiminase, tying the diverse disciplines of science together. His Pyridoxal research is multidisciplinary, incorporating perspectives in Tryptophan and Schiff base.
The scientist’s investigation covers issues in Biochemistry, Enzyme, Stereochemistry, Cysteine and Glutathione. His work on Binding site, Structure–activity relationship and Isozyme as part of general Biochemistry study is frequently linked to Dissociation constant, therefore connecting diverse disciplines of science. His work on Sulfate assimilation as part of general Enzyme study is frequently linked to Protonation and Protein-Arginine Deiminase Type-4, therefore connecting diverse disciplines of science.
His study looks at the relationship between Stereochemistry and topics such as Active site, which overlap with Pentapeptide repeat and Cysteine synthase. His work on Cysteine metabolism as part of general Cysteine research is frequently linked to Protein-arginine deiminase, thereby connecting diverse disciplines of science. His study on Glutathione also encompasses disciplines like
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Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium.
P. Burkhard;G. S. Rao;E. Hohenester;E. Hohenester;K. D. Schnackerz.
Journal of Molecular Biology (1998)
Mechanistic deductions from isotope effects in multireactant enzyme mechanisms
Paul F. Cook;W. W. Cleland.
Biochemistry (1981)
pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same.
Paul F. Cook;W. W. Cleland.
Biochemistry (1981)
The α-aminoadipate pathway for lysine biosynthesis in fungi
Hengyu Xu;Babak Andi;Jinghua Qian;Ann H. West.
Cell Biochemistry and Biophysics (2006)
Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions.
Paul F. Cook;John S. Blanchard;W. W. Cleland.
Biochemistry (1980)
Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase.
Paul F. Cook;Norman J. Oppenheimer;W. W. Cleland.
Biochemistry (1981)
Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase.
Paul F. Cook;George L. Kenyon;W. Wallace Cleland.
Biochemistry (1981)
Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium.
Peter Burkhard;Chia-Hui Tai;Camille M. Ristroph;Paul F. Cook.
Journal of Molecular Biology (1999)
Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants.
Chia Hui Tai;Srinivasa R. Nalabolu;Tony M. Jacobson;David E. Minter.
Biochemistry (1993)
pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase.
Paul F. Cook;W. W. Cleland.
Biochemistry (1981)
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