The transaminations of L-tryptophan (L-trp) and of L-phenylalanine (L-phe) are catalysed in vitro by the same non-spec!fic aminotransferase. The transaminations procceed at the same pH (pH 8.5) and temperature (45 C) optima, have parallel increases in activity with addition of the coenzyme pyridoxal phosphate (PRP) and have identical elution characteristics in gel chromatography. The enzyme from pea seedlings has a relatively weak affinity for both amino acids (KM L-trp = 4.16 • 10 -I mmol 1-1; KM L-phe = 2.10 • 10 -1 mmol 1-1). Differences in affinity for a series of keto acids in the pea enzyme were observed, with pyruvate having the strongest and glyoxylate the weakest affinity. Transamination of L-trp and L-phe was demonstrated by enzyme extracts from pea, maize and tomato, but was not detected in kohlrabi. The amino acids L-asparagine (L-asn), L-phe, L-lysine (L-lys), L-methionine (L-met) have distinct inhibitory effects on the transamination of L-trp. Indolylacetylaspartate and tryptophol were shown to be competitive inhibitors. The regulation at the molecular level of L-trp transaminase activity is discussed.The deamination of L-trp or L-phe to indolylpyruvate (IPyA) and phenylpyruvate (PPyA) is usually regarded as the first step of auxin biosynthesis in higher plants. It may be catalysed by several systems among which L-tryptophan aminotransferase (TAT) has been most frequently investigated (