Man derives 70% of his dietary requirement of protein directly from the grains of cereals and legumes. These sources are respectively deficient in lysine (and secondarily threonine) and methionine and much effort is being devoted to their improvement1. All three amino acids are derived from aspartate via a common metabolic pathway (Fig. 1) in which the first reaction catalysed by aspartate kinase is a key regulatory step limiting their production. In microorganisms, regulation of aspartate kinase occurs by a variety of mechanisms, commonly involving feedback inhibition of one or more isoenzymes by Lys plus Thr, Lys alone or Thr alone2. On the other hand, Met control of this step does not seem to conform to a general pattern. Met represses, but does not inhibit aspartate kinase II of Escherichia coli; in other species Met can enhance or modify the effects of Lys or Thr3. Similarly, varied controls involving Lys and Thr have been reported for the enzymes from higher plants4 with only one report of an effect of Met5. In contrast to these previous results, we suggest here that the methionine derivative (S)-S-adenosyl-L-methione (AdoMet) is an important regulator of the Lys-sensitive aspartate kinase of higher plants, and that this regulatory mechanism is highly conserved. There is thus a major synergistic interaction of the two nutritionally deficient amino acids Lys and Met to inhibit their own syntheses at the primary regulatory step in the pathway.
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