Threonine inhibition of the aspartokinase-homoserine dehydrogenase I of Escherichia coli. Stopped-flow kinetics and the cooperativity of inhibition of the homoserine dehydrogenase activity
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00610a015
Cited by 9 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. Homoserine Dehydrogenase-I (Escherichia coli): Action of Monovalent Ions on Catalysis and Substrate Association-Dissociation;Archives of Biochemistry and Biophysics;1993-03
2. Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I. Equilibrium isotope exchange kinetics.;Journal of Biological Chemistry;1993-03
3. Hysteresis of plant cell-wall β-glucosidase;Biochemical Journal;1990-07-15
4. Interaction of aspartate and aspartate-derived antimetabolites with the enzymes of the threonine biosynthetic pathway of Escherichia coli.;Journal of Biological Chemistry;1984-12
5. 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
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