Substrate interactions with the α-subunit of the Escherichia coli tryptophan synthase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference29 articles.
1. A Steady-State Kinetic Investigation of the Reaction Mechanism of the Tryptophan Synthetase of Escherichia coli
2. The Tryptophan Synthase from Escherichia coli. An Improved Purification Procedure for the alpha-Subunit and Binding Studies with Substrate Analogues
3. The Binding of Indole to the alpha-Subunit and beta2-Subunit and to the alpha2beta2-Complex of Tryptophan Synthase from Escherichia coli. Identification of a Second Indole-Binding Site on the alpha-Subunit
4. Steady-State Kinetic Studies of the Synthesis of Indoleglycerol Phosphate Catalyzed by the alpha Subunit of Tryptophan Synthase from Escherichia coli. Comparison with the alpha2beta2-Complex
5. The Mechanism of the Synthesis of Indoleglycerol Phosphate Catalyzed by Tryptophan Synthase from Escherichia coli. Steady-State Kinetic Studies
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Tryptophan synthase alpha subunit glutamic acid 49 is essential for activity. Studies with 19 mutants at position 49.;Journal of Biological Chemistry;1987-10
2. Proton nuclear magnetic resonance studies on the wild-type and single amino acid substituted tryptophan synthase .alpha.-subunits;Biochemistry;1987-09-08
3. Effect of a single amino acid substitution on the folding of the .alpha. subunit of tryptophan synthase;Biochemistry;1983-03-15
4. Photoaffinity labeling of the indole sites on the Escherichia coli tryptophan synthase α-subunit;Archives of Biochemistry and Biophysics;1983-02
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