Nepsilon-acyllysine derivatives inhibit aspartokinase in Brevibacterium lactofermentum
1994
Ohsumi, T. (Ajinomoto Co. Inc., Kawasaki, Kanagawa (Japan). Central Research Labs.) | Yoshihara, Y. | Ikeda, S.
Several N-acyllysin derivatives were found to inhibit both aspartokinase and cell growth of Brevibacterium lactofermentum. More than ten carbon chains in the N-acyl group were necessary to inhibit the enzyme. In addition, the methylation of the alpha-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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