The effects of 1 milliolar glyphosate (N-Iphosphonomethyllglycine) upon the activities ofenzymes of aromatic amino acid biosynthesis, partially purified by ion-exchange chromatography from mung bean seedings (Vigna radiata IL.I Wilczek), were examined. Multiple isozyme species of shikimate dehydrogenase, chorismate mutase, and aromatic aminotransferase were separated, and these were all insensitive to inhibition by glyphosate. [271, and tobacco [unpublished data]) are now coming to light. Second, the particular details of reversal of glyphosate inhibition by aromatic acids are variable from organism to organism. In E. coli, all three aromatic amino acids are required for complete reversal (25). In Rhizobium japonicum, the combination of phenylalanine plus tyrosine reversed glyphosate inhibition (18) in contrast to Lemna gibba where phenylalanine alone was adequate for reversal (18). In Euglena gracilis, aromatic amino acids only partially reverse inhibition (40%o) unless the minor pathway products: 4-aminobenzoate, 4-hydroxybenzoate, 2,3-dihydroxybenzoate, and 3,4-dihydroxybenzaldehyde are also present (5).Where partial reversal of inhibition is obtained with either Lphenylalanine alone or L-tyrosine alone, the greatest reversal is usually accomplished by L-phenylalanine. For example, the antagonism of inhibition by L-phenylalanine and L-tyrosine was 41% and 12% in Escherichia coli, and 27% and 3% in Chlamydomonas reinhardii (15). Qualitatively, it was found that L-phenylalanine was a better partial antagonist of glyphosate than L-tyrosine in suspension cultures of both carrot and soybean (15)