Plant and Cell Physiology, 1986, Vol. 27, No. 4 607-617
© 1986
Article |
Growth and Aspartate Kinase Activity in Wheat Cell Suspension Culture: Effects of Lysine Analogs and Aspartate-Derived Amino Acids
1Research Center for Cell and Tissue Culture, Faculty of Agriculture, Kyoto University Kyoto 606, Japan
2Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo Tokyo 113, Japan
The effects of lysine analogs and aspartate-derived amino acids on the growth of wheat cell suspension culture were studied. S-(2-Aminoethyl)-L-cysteine (AEC),
-hydroxylysine (DHL) and trans-lysene caused complete growth inhibition at 1.0 mM. The growth inhibition of lysine analogs were, in the order of decreasing effectiveness; AEC
DHL, trans-lysene>oxalysine, homolysine and lysyne. cis-Lysene and methyllysine were not inhibitory even at concentrations of 10 mM. Lysine effectively relieved growth inhibition induced by the lysine analogs. Lysine plus threonine showed concerted inhibition, which was relieved by the addition of methionine.
Activity of aspartate kinase extracted from wheat cell suspension culture was strongly inhibited by L-lysine; 0.75 to 1 mM of lysine was required for half-maximal inhibition. Threonine and methionine, individually or in combination with lysine, showed no inhibitory effect on the enzyme activity. S-Adenosylmethionine, when added with lysine in equimolar concentrations, enhanced the feedback inhibition by lysine, lowering the concentration of lysine for half-maximal inhibition to 0.13 mM. The aspartate kinase isolated from the cells cultured in the presence of 5 mM lysine did not differ in regulatory properties from the enzyme from the cells cultured without lysine. AEC at 5 mM inhibited the enzyme activity by 50%. Other lysine analogs were not inhibitory to the enzyme activity even at 10 mM.
Growth inhibition of wheat suspension culture by aspartate-derived amino acids and lysine analogs were discussed in relation to their inhibitory effects on aspartate kinase activity.
(Received October 25, 1985; Accepted February 26, 1986)
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