The study of indole-3-acetic acid synthesis has undergone something of a revival recently in an attempt to understand the control of IAA levels. Results are, however, contradictory with three separate hypotheses emerging. Our own work supports older evidence for L-tryptophan as the IAA precursor and appears to simplify the metabolism of tryptophan to IAA. Work comparing incorporation of 2H from 2H2O into IAA, tryptophan, tryptamine and indole-3-pyruvate in tomato shoots showed that the indole-3-pyruvate became labelled at a rate compatible with it being the sole intermediate between tryptophan and indole-3-acetaldehyde. Results also showed that tryptamine was not involved in IAA synthesis although it was present. Indole-3-acetaldoxime was not detected in tomato shoots. An aromatic aminotransferase able to catalyse the synthesis of indole-3-pyruvate has been purified from mung beans. This enzyme was separated from aspartate aminotransferase and is fairly specific for aromatic L-amino acids. Other work, however, has implicated D-tryptophan as a more direct precursor than the L-enantiomer. A D-tryptophan aminotransferase has been isolated from dark grown pea seedlings. Finally, other recent work has indicated the existence of an alternative biosynthetic route to IAA which does not involve tryptophan. These results are reviewed in this paper and the apparent contradictions between them discussed.