Lysine-sensitive aspartokinase of Escherichia coli K12. Synergy and autosynergy in an allosteric V system
- 7 September 1976
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 15 (18) , 4053-4058
- https://doi.org/10.1021/bi00663a021
Abstract
The interactions of the lysine-sensitive aspartokinase of E. coli K12 with lysine and leucine, as evidenced in the inhibition and binding curves, are well explained by the equations of an allosteric V model. Mathematical treatments of such a model lead to new linearized plots. These representations are applied to experimental results and allow the direct determination of some parameters of the model (equilibrium constant L'' and leucine Kd. The other parameters are obtained by an optimization method. The theoretical curves drawn according to this model account for the synergistic inhibition between lysine and leucine and for the role of the 2 nonequivalent lysine binding sites (autosynergy).This publication has 6 references indexed in Scilit:
- Two aspartokinases from Escherichia coli. Nature of the inhibition and molecular changes accompanying reversible inactivationBiochemistry, 1968
- MULTIVALENT FEEDBACK INHIBITION OF ASPARTOKINASE IN BACILLUS POLYMYXA .2. EFFECT OF NONPOLAR L-AMINO ACIDS1968
- Regulation by methionine of the synthesis of third aspartokinase and of a second homoserine dehydrohenase in Escherichia coli K 12Biochimica et Biophysica Acta (BBA) - General Subjects, 1967
- The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coliBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*Biochemistry, 1966
- Effets inhibiteurs cooperatifs de la L-lysine avec d’autres amino acides sur une aspartokinase de Escherichia coliBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965