Dependency on Serine Concentration of the Activity of Tryptophan Synthase. Cooperative Properties
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm2.1981.362.2.1567/pdf
Reference15 articles.
1. The 8 protein of Escherichia coli tryptophan synthetase II. New β-elimination and β-replacement reactions
2. Substrate interactions with the α-subunit of the Escherichia coli tryptophan synthase
3. The spatial organization of the active sites of the bifunctional oligomeric enzyme tryptophan synthase: Cross-linking by a novel method
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1. The Catalytic Mechanism of Tryptophan Synthase from Escherichia coli;European Journal of Biochemistry;2005-03-03
2. The Mechanism of Binding of L-Serine to Tryptophan Synthase from Escherichia coli;European Journal of Biochemistry;2005-03-03
3. Evidence for two conformers of the beta subunit of tryptophan synthase in solution;Journal of Biological Chemistry;1992-11
4. Allosteric Interactions Coordinate Covalent Steps in Catalysis and Modulate Indole Transfer Between the α- and β-Sites of the Tryptophan Synthase Bienzyme Complex;Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors;1991
5. Characterization of the reaction of L-serine and indole with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy;Biochemistry;1986-05-01
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