Threonine inhibition of the aspartokinase-homoserine dehydrogenase I of Escherichia coli. Stopped-flow kinetics and the cooperativity of inhibition of the homoserine dehydrogenase activity
- 22 August 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (17) , 3517-3522
- https://doi.org/10.1021/bi00610a015
Abstract
No abstract availableThis publication has 5 references indexed in Scilit:
- Interaction of substrates and inhibitors with the homoserine dehydrogenase of kinase-inactivated aspartokinase IBiochemistry, 1977
- Fluorescence energy transfer between heterologous active sites of affinity-labeled aspartokinase of Escherichia coliBiochemistry, 1977
- Cobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adductsBiochemistry, 1976
- The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K-12. Incubation of the Enzyme in Alkaline Conditions: Dissociation and Disulfide-Bridge FormationEuropean Journal of Biochemistry, 1976
- The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coliBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966