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.-Reference-Cited by-同舟云学术

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.

Published:1992-01 Issue:1 Volume:267 Page:526-541
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Zhao G P,Somerville R L

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference72 articles.

1. Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the .beta.2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimurium

2. A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana.

3. Charon Phages: Safer Derivatives of Bacteriophage Lambda for DNA Cloning

4. Analysis in vivo of factors affecting the control of transcription initiation at promoters containing target sites for Trp repressor

5. Trp repressor protein controls its own structural gene

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