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. 1971 Dec;108(3):1129–1134. doi: 10.1128/jb.108.3.1129-1134.1971

Regulation of Two Aspartokinases in Bacillus subtilis

Michael L Hampton a, Neil G McCormick a,1, Nancy C Behforouz a,2, Ernst Freese a
PMCID: PMC247196  PMID: 5003173

Abstract

When grown on minimal glucose medium, transformable Bacillus subtilis strains contained two distinct aspartokinases (ATP:l-aspartate 4-phosphotransferase, EC 2.7.2.4). One of these enzymes was inhibited by l-lysine (Lys), whereas the other was insensitive to inhibition but was activated by l-leucine. None of the other amino acids tested had any effect, and the addition of l-threonine did not enhance the inhibition by Lys, in contrast to the concerted inhibition observed for other bacilli. At the end of exponential growth, the Lys-sensitive aspartokinase activity decreased, whereas the Lys-insensitive activity remained relatively constant throughout the stationary phase. The two activities were separated by (NH4)2SO4 fractionation and Sephadex G-200 chromatography. Growth in the presence of Lys reduced the specific activity of aspartokinase by about 50% and eliminated the inhibition by Lys. In extracts of these cells, only Lys-insensitive activity was found upon (NH4)2SO4 fractionation and Sephadex G-200 chromatography. Lys apparently repressed the synthesis of the Lys-sensitive enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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