Abstract
The enzymic activation of amino acid in various plant extracts was studied by means of the exchange of ATP with inorganic pyrophosphate. In extracts of pea seedlings, leucine, tyrosine, valine, tryptophan, isoleucine, cysteine, and methionine were the only amino acids that stimulated the PP-ATP exchange reaction. The exchange reaction is about 50% inhibited by KF. The properties of the exchange reaction in plants are discussed in relation to the similar reaction previously described in bacteria.
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