Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate.-Reference-Cited by-同舟云学术

Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate.

Published:1983-11 Issue:21 Volume:258 Page:12940-12946
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Broglie K E,Takahashi M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference24 articles.

1. Structure, Function, and Possible Origin of a Bifunctional Allosteric Enzyme,Escherichia ColiAspartokinase I-Homoserine Dehydrogenase

2. Multifunctional Proteins;Cohen,1980

3. 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

4. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli

5. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. Intra and Intersubunit Interactions between the Catalytic Regions of the Bifunctional Enzyme

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