Substrate interactions with the α-subunit of the Escherichia coli tryptophan synthase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference34 articles.
1. Association of the α and β2 Subunits of the Tryptophan Synthetase of Escherichia coli
2. Subunit structure of the tryptophan synthetase of Escherichia coli
3. A study of the catalytic properties of Escherichia coli tryptophan synthetase, a two-component enzyme
4. A new thiol-dependent transamination reaction catalyzed by the B protein of Escherichia coli tryptophan synthetase
Cited by 9 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. Affinities of phosphorylated substrates for theE. coli tryptophan synthase α-subunit: Roles of Ser-235 and helix-8′ dipole;Proteins: Structure, Function, and Genetics;1995-02
2. Proton nuclear magnetic resonance studies on the wild-type and single amino acid substituted tryptophan synthase .alpha.-subunits;Biochemistry;1987-09-08
3. 5-Azidoindole binding to the Escherichia coli tryptophan synthase α2β2 complex;Archives of Biochemistry and Biophysics;1984-10
4. Photoaffinity labeling of the indole sites on the Escherichia coli tryptophan synthase α-subunit;Archives of Biochemistry and Biophysics;1983-02
5. A critical reexamination of the continous spectrophotometric assay for adenosine deaminase;Analytical Biochemistry;1982-05
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