Shoots of barley seedlings when fed D-phenylalanine convert the amino acid to N-malonylphenylalanine. Some N-acetylphenylalanine is obtained at the same time but this may be an artifact of the isolation procedure since it is readily formed by decarboxylation of the malonylphenylalanine. Feeding experiments with the D- and L-isomers of phenylalanine, valine, leucine, isoleucine, tyrosine, tryptophan, alanine, and glutamic acid showed that barley shoots form the malonyl derivative from all the D-isomers whereas little, if any, is formed from the L-isomers. Similar experiments with phenylalanine and leucine isomers, using seven different plant species, showed that the ability to conjugate the D-isomers (but not the L-isomers) was found in all of the plants tested. It was also observed that the ether-soluble acidic conjugates of a variety of amino acids, possibly malonyl derivatives, occur widely throughout the plant kingdom.
The estimation of the leucine isomers in protein hydrolysates by infrared analysis
