The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of the enzyme: threonine binding and inhibition are functionally dissociable.-Reference-Cited by-同舟云学术

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of the enzyme: threonine binding and inhibition are functionally dissociable.

Published:1978-04 Issue:8 Volume:253 Page:2754-2757
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fontan E.,Truffa-Bachi P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits

2. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. Subunit Structure of the Protein Catalyzing the Two Activities

3. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. A Study of the Allosteric Equilibrium

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

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Reversible dissociation of aspartokinase I/homoserine dehydrogenase I from Escherichia coli K 12. The active species is the tetramer;European Journal of Biochemistry;1985-09

2. Interaction of aspartate and aspartate-derived antimetabolites with the enzymes of the threonine biosynthetic pathway of Escherichia coli.;Journal of Biological Chemistry;1984-12

3. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of a unique cysteine induces a conformational change of the enzyme.;Journal of Biological Chemistry;1978-04