Assignment of the ends of the β-chain of E. coli tryptophan synthase to the F1 and F2 domains
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12. The Two Catalytic Activities Are Carried by Two Independent Regions of the Polypeptide Chain
2. Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.
3. Isolation and characterization of independently folding regions of the β chain of Escherichia coli tryptophan synthetase
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1. Structural Basis for Catalysis by Tryptophan Synthase;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Tryptophan Synthase: Structure, Function, and Subunit Interaction;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Importance of Residues 2–9 in the Immunoreactivity, Subunit Interactions, and Activity of the β2 Subunit of Escherichia coli Tryptophan Synthase;Journal of Biological Chemistry;1995-03
4. An amino acid switch (Gly281–>Arg) within the “hinge” region of the tryptophan synthase beta subunit creates a novel cleavage site for the OmpT protease and selectively diminishes affinity toward a specific monoclonal antibody;Journal of Biological Chemistry;1993-07
5. Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.;Journal of Biological Chemistry;1992-01
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