Threonine-sensitive aspartokinase from Escherichia coli. Magnetic resonance and binding studies
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00746a002
Reference26 articles.
1. Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments
2. Transition Metal Binding in DNA Solutions
3. Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits
4. Threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli K12. Evidence for a cooperative tetramer
Cited by 13 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. Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I. Equilibrium isotope exchange kinetics.;Journal of Biological Chemistry;1993-03
2. Internal homologies in the two aspartokinase-homoserine dehydrogenases of Escherichia coli K-12.;Proceedings of the National Academy of Sciences;1984-05-01
3. Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate.;Journal of Biological Chemistry;1983-11
4. Characterization of proteolysis fragments of aspartokinase I: homoserine dehydrogenase I. Fluorescence and circular dichroism studies.;Journal of Biological Chemistry;1983-11
5. Threonine inhibition of the aspartokinase-homoserine dehydrogenase I of Escherichia coli. Threonine binding studies;Biochemistry;1978-08-22
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