Abstract
A single aspartate kinase (ATP: l-aspartate 4-phosphotransferase, EC 2.7.2.4) of Pseudomonas putida has been obtained in a partially purified state. The enzyme is inhibited allosterically by l-lysine and l-threonine individually and is also subject to a concerted feedback inhibition by these amino acids. Some of the properties of the enzyme, the kinetic constants and approximate molecular weight, the type of inhibition by l-lysine and l-threonine and their concerted feedback inhibition, the effect of lysine and threonine analogues on enzyme activity and the protection of the enzyme by the inhibitors against thermal inactivation, are described. Investigation of regulation by feedback inhibition and repression revealed that enzyme synthesis is not only repressed when cells are growing in the presence of the inhibitors but that the enzymes synthesized under these conditions is sensitive neither to lysine or threonine nor to their concerted feedback inhibition. The regulation and some other particularities of the enzyme are discussed.
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