Interactions of tryptophan synthetase subunits in Escherichia coli containing mutationally altered beta2 subunits.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. A Mutational Alteration of the Tryptophan Synthetase of Escherichia coli
2. MUTANTS OF ESCHERICHIA COLI DEFECTIVE IN THE B PROTEIN OF TRYPTOPHAN SYNTHETASE I. SELECTION AND CLASSIFICATION
3. MUTANTS OF ESCHERICHIA COLI DEFECTIVE IN THE B PROTEIN OF TRYPTOPHAN SYNTHETASE. II. INTRAGENIC POSITION
4. MUTANTS OF ESCHERICHIA COLI DEFECTIVE IN THE B PROTEIN OF TRYPTOPHAN SYNTHETASE. III. INTRAGENIC CLUSTERING
5. Association of the α and β2 Subunits of the Tryptophan Synthetase of Escherichia coli
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1. 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
2. A radioactive assay for the physiological activity of the tryptophan synthetase α subunit in crude extracts of Escherichia coli;Biochimie;1990-12
3. Missense and nonsense suppressors can correct frameshift mutations;Biochimie;1989-06
4. Reversion of trpA nonsense mutations by deletion of the chain-termination codons;Biochimie;1989-06
5. A simple structural feature is a major determinant of the identity of a transfer RNA;Nature;1988-05
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