Energetic adaptation of ligand binding to subunit structure of tryptophan synthase from Escherichia coli
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00316a016
Reference31 articles.
1. Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli
2. SERINE DEAMINATION BY THE B PROTEIN OF ESCHERICHIA COLI TRYPTOPHAN SYNTHETASE
3. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit
4. Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme
5. Structural and Functional Roles of the Cysteine Residues in the α Subunit of the Escherichia coli Tryptophan Synthetase
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1. Kinetic and thermodynamic study of the reaction of pyridoxal 5′-phosphate withL-tryptophan;Journal of Physical Organic Chemistry;2005
2. Schiff’s Bases Formed between Pyridoxal 5′-Phosphate and 4-Aminobutanoic Acid. Kinetic and Thermodynamic Study;Bulletin of the Chemical Society of Japan;2003-03
3. Regulation of Tryptophan Synthase by Temperature, Monovalent Cations, and an Allosteric Ligand. Evidence from Arrhenius Plots, Absorption Spectra, and Primary Kinetic Isotope Effects;Biochemistry;2000-03-29
4. A thermodynamic investigation of reactions catalyzed by tryptophan synthase;Biophysical Chemistry;1998-07
5. Structural Characteristics of Brain Glutamate Decarboxylase in Relation to Its Interaction and Activation;Archives of Biochemistry and Biophysics;1998-01
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