Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Nε-Acyllysine Derivatives Inhibit Aspartokinase in Brevibacterium lactofermentum
Tsuyoshi OhsumiYasuhiko YoshiharaShigeho Ikeda
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1994 Volume 58 Issue 7 Pages 1351-1352

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Abstract
Several Nε-acyllysine derivatives were found to inhibit both aspartokinase and cell growth of Brevibacterium lactofermentum. More than ten carbon chains in the Nε-acyl group were necessary to inhibit the enzyme. In addition, the methylation of the α-amino group was not directly involved in the inhibitory activity, but it was related to inhibition by its effect on enhancing the molecules'solubility in water. The inhibition of cell growth was not reversed by individual addition of lysine, threonine, or methionine, but was reversed by the simultaneous addition of all three amino acids.
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