The role of the hinge region of the beta 2-subunit in beta-replacement specificity of tryptophan synthase from Escherichia coli. Analysis of proteolytically modified beta species cleaved by endoproteinase Glu-C-Reference-Cited by-同舟云学术

The role of the hinge region of the beta 2-subunit in beta-replacement specificity of tryptophan synthase from Escherichia coli. Analysis of proteolytically modified beta species cleaved by endoproteinase Glu-C

Published:1994-04 Issue:13 Volume:269 Page:9783-9789
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Linkens H.J.,Bartholmes P.,Kaufmann M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. A Rapid Method for Preparing Crystalline b2 Subunit of Tryptophan Synthetase of Escherichia coli in High Yield

2. 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

3. Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.

4. Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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1. Multifunctional Tryptophan-synthesizing Enzyme;Journal of Biological Chemistry;1997-04

2. Exchange of K+ or Cs+ for Na+ Induces Local and Long-Range Changes in the Three-Dimensional Structure of the Tryptophan Synthase α2β2 Complex;Biochemistry;1996-01-01